G6PD Deficiency Bibliography ***Data was generously offered to the Favism Site by Ernest Beutler, M.D.

, who h as been working in this field for the past 40 years and is currently at the Depa rtment of Molecular and Experimental Medicine, Research Institute of Scripps Cli nic*** * Lajos, S. and Istvan, V. A vorosversejtek glucose-6-phosphat dehydrogenase enzymdefektusa. Orv.Hetil.:2318-2321, 0. * Mareni, C., D'Urso, M., and Luzzatto, L. Turnover of genetic variants of glucose 6-phosphate dehydrogenase in human fibroblasts. Unpublished , 0. * Haas, E. The effect of atabrine and quinine on isolated respiratory enzymes. J.Biol.Chem. 135:321-331, 1914. * Muehlens, P. Die behandlung der naturlichen menschlichen malaria-infektion mit plasmochin. Naturwissenschaften 14:1162-1166, 1926. * Cordes, W. Observations on the toxic effect of plasmochin. United Fruit Co.(Med.Dept.), Annual Report 16:62-67, 1927. * Warburg, C., Kubowitz, F., and Christian, W. ber die wirkung von Phenylhydrazine und Phenylhydroxlamin auf den Stoffwechsel der roten Blutzellen (Methode zur Messung des Stoffwechsels roter Blutzellen). Biochem.Z. 242:170-205, 1931. * Negelein, E. and Haas, E. ber die Wirkungsweise des Zwischenferments. Biochem.J. 282:206-220, 1935. * Earle, D.P.J., Bigelow, F.S., Zubred, C.G., and Kane, C.A. Studies on the chemotherapy on the human malarias. IX. Effect of primaquine on the blood cells of man. J.Clin.Invest. 27:121-129, 1948. * Zuelzer, W.W. and Apt, L. Acute hemolytic anemia due to naphthalene poisoning. JAMA 141:185-190, 1949. * Horecker, B.L. and Smyrniotis, P.Z. Phosphogluconic acid dehydrogenase from yeast. J.Biol.Chem. 193:371-381, 1951. * Alving, A.S., Arnold, J., and Robinson, D.H. Status of primaquine. I. Mass therapy of subclinical vivax malaria with primaquine. JAMA 149:1558-1562, 1952. * Cori, O. and Lipmann, F. The primary oxidation product of enzymatic glucose-6-phosphate oxidation. J.Biol.Chem. 194:417-425, 1952. * Glock, G.E. and McLean, P. Further studies on the properties and assay of glucose-6-phosphate dehydrogenase, and 6-phosphogluconate dehydrogenase of rat liver. Biochem.J. 55:400-408, 1953. * Horecker, B.L. and Smyrniotis, P.Z. Reversibility of glucose-6-phosphate oxidation. Biochim.Biophys.Acta 12:98-102, 1953. * Jones, R.J., Jackson, L.S., Di Lorenzo, A., Marx, R.L., Levy, B.L., Kenny, E.C., Gilbert, M., Johnston, N.N., and Alving, A.S. Korean vivax malaria. III. Curative effect and toxicity of primaquine in doses from 10-30 mg/d. Am.J.Trop.Med.Hyg. 2:977-982, 1953. * Archambeault, C.P. Mass antimalarial therapy in veterans returning from Korea. JAMA 154:1411-1415, 1954. * Beutler, E., Dern, R.J., and Alving, A.S. The hemolytic effect of primaquine. III. A study of primaquine-sensitive erythrocytes. J.Lab.Clin.Med. 44:177-184, 1954. Notes: (B8). * Beutler, E., Dern, R.J., and Alving, A.S. The hemolytic effect of primaquine. IV. The relationship of cell age to

hemolysis. J.Lab.Clin.Med. 44:439-442, 1954. Notes: (B9). * Dern, R.J., Weinstein, I.M., Le Roy, G.V., Talmage, D.W., and Alving, A.S. The hemolytic effect of primaquine. I. The localization of the drug- induced hemolytic defect in primaquine-sensitive individuals. J.Lab.Clin.Med. 43:303-309, 1954. * Dern, R.J., Beutler, E., and Alving, A.S. The hemolytic effect of primaquine. II. The natural course of the hemolytic anemia and the mechanism of its self-limited character. J.Lab.Clin.Med. 44:171-175, 1954. Notes: (B7). * Dern, R.J., Beutler, E., Flanagan, C.L., and Alving, A.S. Studies of the acute hemolytic anemia induced by certain aniline derivatives and related compounds. J.Lab.Clin.Med. 44:788, 1954. Notes: (B13). * Beutler, E., Dern, R.J., and Alving, A.S. The hemolytic effect of primaquine. VI. An in vitro test for sensitivity of erythrocytes to primaquine. J.Lab.Clin.Med. 45:40-50, 1955. Notes: (B15). * Beutler, E., Dern, R.J., Flanagan, C.L., and Alving, A.S. The hemolytic effect of primaquine. VII. Biochemical studies of drug-sensitive erythrocytes. J.Lab.Clin.Med. 45:286-295, 1955. Notes: (B16). * Dern, R.J., Beutler, E., and Alving, A.S. The hemolytic effect of primaquine. V. Primaquine sensitivity as a manifestation of a multiple drug sensitivity. J.Lab.Clin.Med. 45:30-39, 1955. Notes: (B14). * Flanagan, C.L., Beutler, E., Dern, R.J., and Alving, A.S. Biochemical changes in erythrocytes during hemolysis induced by aniline derivatives. J.Lab.Clin.Med. 46:814, 1955. Notes: (B23). * Glaser, L. and Brown, D.H. Purification and properties of D-glucose-6-phosphate dehydrogenase. J.Biol.Chem. 216:67-79, 1955. * Beutler, E. In vitro studies of the stability of red cell glutathione: A new test for drug sensitivity. J.Clin.Invest. 35:690-691, 1956. Notes: (B24). * Carson, P.E., Flanagan, C.L., Ickes, C.E., and Alving, A.S. Enzymatic deficiency in primaquine-sensitive erythrocytes. Science 124:484-485, 1956. * West, M. and Zimmerman, H.J. Hemolytic anemia in patient receiving nitrofurantoin (furadantin). JAMA 162:637-639, 1956. * Beutler, E. The glutathione instability of drug-sensitive red cells. A new method for the in vitro detection of drug-sensitivity. J.Lab.Clin.Med. 49:84-95, 1957. Notes: (B25). * Beutler, E., Robson, M., and Buttenwieser, E. The mechanism of glutathione destruction and protection in drug-sensitive and non-sensitive erythrocytes. In vitro studies. J.Clin.Invest. 36:617-628, 1957. Notes: (B26). * Beutler, E. Hemolytic anemia. JAMA 164:1381-1382, 1957. Notes: (B28). * Browne, E.A. The inheritance of an intrinsic abnormality of the red blood cell predisposing to drug-induced hemolytic anemia. Johns Hopkins Med.J. 101:115-118, 1957. * Kimbro, E.L.J., Sachs, M.V., and Torbert, J.V. Mechanism of

the hemolytic anemia induced by nitrofurantoin (Furadantin). Johns Hopkins Med.J. 101:245-257, 1957. * Waller, H.D., Lhr, G.W., and Tabatabai, M. Hemolyse und Fehlen von Glucose-6-phosphat-dehydrogenase in roten Blutzellen (eine Fermentanomalie der Erythrocyten). Klin.Wochenschr. 35:1022-1027, 1957. * Zinkham, W.H. and Childs, B. Effect of naphthalene derivatives on glutathione metabolism of erythrocytes from patients with naphthalene hemolytic anemia. J.Clin.Invest. 36:938-939, 1957. * Alving, A.S., Kellermeyer, R.W., Tarlov, A., Schrier, S., and Carson, P.E. Biochemical and genetic aspects of primaquine sensitive anemia. Ann.Intern.Med. 49:240-248, 1958. * Childs, B., Zinkham, W., Browne, E.A., Kimbro, E.L., and Torbert, J.V. A genetic study of a defect in glutathione metabolism of the erythrocyte. Johns Hopkins Med.J. 102:21-37, 1958. * Dawson, J.P., Thayer, W.W., and Desforges, J.F. Acute hemolytic anemia in the newborn infant due to naphthalene poisoning. Report of two cases with investigation into the mechanism of the disease. Blood 13:1113-1125, 1958. * Flanagan, C.L., Schrier, S.L., Carson, P.E., and Alving, A.S. The hemolytic effect of primaquine VIII. The effect of drug administration on parameters of primaquine sensitivity. J.Lab.Clin.Med. 51:600-608, 1958. * Kellermeyer, R.W., Tarlov, A.R., Schrier, S.L., and Alving, A.S. Hemolytic effect of commonly used drugs on erythrocytes deficient in glucose-6-phosphate dehydrogenase. J.Lab.Clin.Med. 52:827-828, 1958. * Lhr, G.W. and Waller, H.D. Hemolytische erythrocytopathie durch fehlen von glukose-6-phosphat- dehydrogenase in roten blutzellen als dominant vererbliche krankheit. Klin.Wochenschr. 36:865-869, 1958. * Marks, P.A. Red cell glucose-6-phosphate and 6-phosphogluconic dehydrogenases and nucleoside phosphorylase. Science 127:1338-1339, 1958. * Marks, P.A., Johnson, A.B., and Hirschberg, E. Effect of age on the enzyme activity in erythrocytes. Proc.Natl.Acad.Sci.USA 44:529-536, 1958. * Marks, P.A. and Johnson, A.B. Relationship between the age of human erythrocytes and their osmotic resistance: A basis for separating young and old erythrocytes. J.Clin.Invest. 37:1542-1548, 1958. * McGovern, J.J., Isselbacher, K., Rose, P.J., and Grossman, M.S. Observations on the glutathione (GSH) stability of red blood cells. Am.J.Dis.Child. 96:502, 1958. * Newton, W.A.J. and Bass, J.C. Glutathione sensitive chronic non-spherocytic hemolytic anemia. Am.J.Dis.Child. 96:501-502, 1958. * Sansone, G. L'anemia emolitica acuta de ingestione accidentale di naftalina nel bambino. Haematologica (Latina) 1:45-60, 1958. * Sansone, G. and Segni, G. Difetto biochimico eritrocitario, a carattere genetico, in un bambino con anemia emolitica acuta da naftalina. Boll.Soc.Ital.Biol.Sper. 34:615-617, 1958. * Sansone, G. and Segni, G. L'anemia emolitica acuta da sulfamide e quella da pas: Differenze patogenetiche. Boll.Soc.Ital.Biol.Sper. 34:1556-1558, 1958. * Schrier, S., Kellermeyer, R., and Alving, A.S. Coenzyme studies in primaquine-sensitive erythrocytes.

Proc.Soc.Exp.Biol.Med. 99:354-356, 1958. * Schrier, S.L., Kellermeyer, R.W., Carson, P.E., Ickes, C.E., and Alving, A.S. The hemolytic effect of primaquine (IX. Enzymatic abnormalities in primaquine-sensitive erythrocytes). J.Lab.Clin.Med. 52:109-117, 1958. * Szeinberg, A., Ramot, B., Sheba, C., Adam, A., Halbrecht, I., Rikover, M., Wishnievsky, S., and Rabau, E. Glutathione metabolism in cord and newborn infant blood. J.Clin.Invest. 37:1436-1441, 1958. * Szeinberg, A., Sheba, C., and Adam, A. Selective occurrence of glutathione instability in red blood corpuscles of the various Jewish tribes. Blood 13:1043-1053, 1958. * Zinkham, W.H. and Childs, B. A defect in GSH metabolism in erythrocytes from patients with a naphthalene-induced hemolytic anemia. Pediatrics 22:461-471, 1958. * Beutler, E., Yeh, M.K.Y., and Necheles, T. Incidence of the erythrocytic defect associated with drug sensitivity among Oriental subjects. Nature 183:684-685, 1959. Notes: (B42). * Beutler, E. The hemolytic effect of primaquine and related compounds. A review. Blood 14:103-139, 1959. Notes: (B39). * Desforges, J.F., Thayer, W.W., and Dawson, J.P. Hemolytic anemia induced by sulfoxone therapy, with investigations into the mechanisms of its production. Am.J.Med. 27:132-136, 1959. * Desiderio, V.C. and Beem, J.R. Antihypertensive properties of furazolidone. Proc.Soc.Exp.Biol.Med. 100:343-346, 1959. * Heller, P. and Weinstein, H. Aldolase, isocitric dehydrogenase and malic dehydrogenase in glucose-6- phosphate dehydrogenase deficient erythrocytes. J.Lab.Clin.Med. 54:824-825, 1959. * Houston, I.B. and Barlow, A.M. Acute haemolytic anaemia and methaemoglobinuria produced by phenacetin. Lancet 2:1062-1065, 1959. * Kirkman, H.N. Glucose-6-phosphate dehydrogenase and human erythrocytes. Nature 184:1291-1292, 1959. * Marks, P.A., Gross, R.T., and Hurwitz, R.E. Gene action in erythrocyte deficiency of glucose-6-phosphate dehydrogenase: Tissue enzyme-levels. Nature 183:1266-1267, 1959. * Marks, P.A. and Gross, R.T. Erythrocyte glucose-6-phosphate dehydrogenase deficiency: Evidence of differences between negroes and caucasians with respect to this genetically determined trait. J.Clin.Invest. 38:2253-2262, 1959. * Marks, P.A. and Gross, R.T. Further characterization of the enzymatic defect in erythrocyte glucose-6-phosphate dehydrogenase deficiency. A genetically determined trait. J.Clin.Invest. 38:1023-1024, 1959. * Ramot, B., Szeinberg, A., Adam, A., Sheba, C., and Gafni, D. A study of subjects with erythrocyte glucose-6-phosphate dehydrogenase deficiency: I. Investigation of platelet enzymes. J.Clin.Invest. 38:1659-1661, 1959. * Ramot, B., Fisher, S., Szeinberg, A., Adam, A., Sheba, C., and Ganni, D. A study of subjects with erythrocyte glucose-6-phosphate dehydrogenase deficiency. II. Investigation of leukocyte enzymes. J.Clin.Invest. 38:2234-2237, 1959. * Schrier, S.L., Kellermeyer, R.W., Carson, P.E., Alving, A.S., and Ickes, C.E. The hemolytic effect of primaquine. IX. Enzymatic abnormalities in primaquine-sensitive erythrocytes. J.Lab.Clin.Med. 54:232-240, 1959. * Segni, G. Su due casi di ittero nucleare in neonati con

difetto enzimatico eritrocitario. Minerva Pediatr. 11:1420-1426, 1959. * Shahidi, N.T. and Diamond, L.K. Enzyme deficiency in erythrocytes in congenital nonspherocytic hemolytic anemia. Pediatrics 24:245-253, 1959. * Sonnet, J., Vandepitte, J., and Haumont, A. Anemie hemolytique par la nitrofurazone revelatrice d'une deficience globulair en glucose-6-phosphate dehydrogenase. Ann.Soc.Belg.Med.Trop. 39:691-702, 1959. * Szeinberg, A., Pras, M., Sheba, C., Adam, A., and Ramot, B. The hemolytic effect of various sulfonamides on subjects with a deficiency of glucose-6-phosphate dehydrogenase of erythrocytes. Isr.J.Med.Sci. 18:176-183, 1959. * Szeinberg, A., Pras, M., Sheba, C., Adam, A., and Ramot, B. The hemolytic effect of various sulfonamides on subjects with a deficiency of glucose-6-phosphate dehydrogenase of erythrocytes. Isr.Med.J. 18:176, 1959. * Szeinberg, A., Adam, A., Ramot, B., Sheba, C., and Myers, F. The incorporation of isotopically labelled glycine into the glutathione of erythrocytes with glucose-6-phosphate dehydrogenase deficiency. Biochim.Biophys.Acta 36:65, 1959. * Szeinberg, A., Adam, A., Myers, F., Sheba, C., and Ramot, B. A hematological survey of industrial workers with enzyme-deficient erythrocytes. AMA Arch.Ind.Health 20:510-516, 1959. * Walker, D.G. and Bowman, J.E. Glutathione stability of the erythrocytes in Iranians. Nature 184:1325, 1959. * Zinkham, W.H. An in vitro abnormality of glutathione metabolism in erythrocytes from normal newborns: Mechanism and clinical significance. Pediatrics 23:18-23, 1959. * Zinkham, W.H. and Lenhard, R.E. Metabolic abnormalities of erythrocytes from patients with congenital nonspherocytic hemolytic anemia. J.Pediatr. 55:319-336, 1959. * Zinkham, W.H. and Lenhard, R.E.J. Observations on the significance of primaquine sensitive erythrocytes in patients with congenital nonspherocytic hemolytic anemia. Am.J.Dis.Child. 98:443-445, 1959. * Adinolfi, M., Bernini, L., Carcassi, U., Latte, B., Motulsky, A.G., Siniscalco, M., and Montalenti, G. Indagini genetiche sulla predisposizione al favismo. I. Il problema ed I metodi. Fluttuazioni stagionali dei livelli di glucoso-6-fosfatodeidrogenasi in sardegna. Interazione con la talassemia al livello fisiologico. Matematiche E.Naturali 28:1-11, 1960. * Allison, A.C. Glucose 6-phosphate dehydrogenase deficiency in red blood cells of East Africans. Nature 186:531-532, 1960. * Alving, A.S., Tarlov, A.R., Brewer, G., Carson, P.E., Kellermeyer, R.W., and Long, W.F. Glucose-6-phosphate dehydrogenase deficiency: Some biological implications. Trans.Assoc.Am.Phys. 73:80, 1960. * Alving, A.S., Johnson, C.F., Tarlov, A.R., Brewer, G.J., Kellermeyer, R.W., and Carson, P.E. Mitigation of the haemolytic effect of primaquine and enhancement of its action against exoerythrocytic forms of the chesson strain of plasmodium vivax by intermittent regimens of drug administration. Bull.WHO 22:621-631, 1960. * Beutler, E. Drug-induced hemolytic anemia (primaquine sensitivity). In: The Metabolic Basis of Inherited Disease, edited by Stanbury, J.B., Wyngaarden, J.B., and Fredrickson, D.S.New York:McGraw-Hill, Inc. 1960,p. 1031-1067. Notes: (B62).

* Beutler, E. Sensitivity to drug-induced hemolytic anemia. A hereditary metabolic disorder of the erythrocyte. Proc.8th Int.Cong.Hematol.Tokyo,Sept.4-10:1101-1106, 1960. Notes: (B89). * Carson, P.E. Glucose-6-phosphate dehydrogenase deficiency in hemolytic anemia. Fed.Proc. 19:995-1006, 1960. * Charles, L.J. Observations on the haemolytic effect of primaquine in 100 Ghanaian children. Ann.Trop.Med.Parasitol. 54:460-470, 1960. * Desforges, J.F., Kalaw, E., and Gilchrist, P. Inhibition of glucose-6-phosphate dehydrogenase by hemolysis inducing drugs. J.Lab.Clin.Med. 55:757-766, 1960. * Doxiadis, S.A., Fessas, P., and Valaes, T. Erythrocyte enzyme deficiency in unexplained kernicterus. Lancet 2:44, 1960. * Gilles, H.M. and Ikeme, A.C. Hemoglobinuria among adult Nigerians due to glucose-6-phosphate dehydrogenase deficiency with drug sensitivity. Lancet 2:889-891, 1960. * Kirkman, H.N., Riley, H.D.J., and Crowell, B.B. Different enzymic expressions of mutants of human glucose-6-phosphate dehydrogenase. Proc.Natl.Acad.Sci.USA 46:938-944, 1960. * Lenzerini, L. and Contu, L. Instability of erythrocytic, reduced glutathione (GSH) in the pathogenesis of icteric-hemoglobinuric favism. Clin.Ther. 32:312-328, 1960. * Lisker, R., Loria, A., and Strygler, I. Anemia hemolitica ligada a la inestabilidad el glutation reducido de los eritrocitos. Prensa Med.Mex. 25:451-457, 1960. * Lisker, R., Loria, A., and Strygler, I. Hemolytic anemia associated to instability of the reduced glutathione of the erythrocyte. Family affected with this defect. Prensa Med.Mex. 25:2-8, 1960. * Marks, P.A. and Banks, J. Inhibition of mammalian glucose-6-phosphate dehydrogenase by steroids. Proc.Natl.Acad.Sci.USA 46:447-452, 1960. * Naylor, J., Rosenthal, I., Grossman, A., Schulman, I., and Hsia, D.Y.Y. Activity of glucose-6-phosphate dehydrogenase in erythrocytes of patients with various abnormal hemoglobins. Pediatrics 26:285-292, 1960. * Panizon, F. Dimostrazione della anomalia enzimatica nel fegato di soggetti con difetto eritrocitario di glucose-6-fosfato deidrogenasi. Boll.Soc.Ital.Biol.Sper. 36:106-108, 1960. * Panizon, F. L'ictere grave du nouveau-ne associe a une deficience en glucose-6-phosphate dehydrogenase. Biol.Neonate 2:167-177, 1960. * Panizon, F. Erythrocyte enzyme deficiency in unexplained kernicterus. Lancet 2:1093, 1960. * Ramot, B., Sheba, C., Adam, A., and Ashkenasi, I. Erythrocyte glucose-6-phosphate dehydrogenase deficient subjects: Enzyme-level in saliva. Nature 185:931, 1960. * Rimon, A., Askenazi, I., Ramot, B., and Sheba, C. Activation of glucose-6-phosphate dehydrogenase of enzyme deficient subjects: 1. Activation by stroma of normal erythrocytes. Biochem.Biophys.Res.Commun. 2:138-141, 1960. * Siniscalco, M., Motulsky, A.G., Latte, B., Bernini, L., and Montalenti, G. Indagnini genetiche sulla predisposizione al favismo. II. Dati familiari: Associazione genica con il daltonismo. Accad.Naz.Dei.Lincei. 28:1-7, 1960. * Smith, G. and Vella, F. Erythrocyte enzyme deficiency in unexplained kernicterus. Lancet 1:1133-1134, 1960. * Sonnet, J. and Michaux, J.L. Glucose-6-phosphate dehydrogenase deficiency , haptoglobin groups, blood groups and

sickle-cell trait in the Bantus of West Belgian Congo. Nature 188:504-505, 1960. * Swarup, S., Ghosh, S.K., and Chatterjea, J.B. Glutathione stability test in haemoglobin E-thalassemia disease. Nature 188:153, 1960. * Szeinberg, A., Kellermann, J., Adam, A., Sheba, C., and Ramot, B. Haemolytic jaundice following aspirin administration to a patient with a deficiency of glucose-6-phosphate dehydrogenase in erythrocytes. Acta Haematol.(Basel) 23:58-64, 1960. * Weatherall, D.J. Enzyme deficiency in haemolytic disease of the newborn. Lancet 2:835-837, 1960. * Zinkham, W.H. Enzyme studies on lenses from persons with primaquine-sensitive erythrocytes. Am.J.Dis.Child. 100:525-526, 1960. * Adam, A. Linkage between deficiency of glucose-6-phosphate dehydrogenase and colour-blindness. Nature 189:686, 1961. * Allison, A.C. and Clyde, D.F. Malaria and glucose-6-phosphate dehydrogenase. BMJ 1:1358, 1961. * Allison, A.C., Charles, L.J., and McGregor, I.A. Erythrocyte glucose-6-phosphate dehydrogenase deficiency in West Africa. Nature 190:1198, 1961. * Allison, A.C. and Clyde, D.F. Malaria in African children with deficient erythrocyte glucose-6-phosphate dehydrogenase. BMJ 1:1346-1349, 1961. * Allison, A.C. and Clyde, D.F. Malaria and glucose-6-phosphate dehydrogenase. BMJ 2:521-522, 1961. * Allison, A.C. Genetic factors in resistance to malaria. Ann.NY Acad.Sci. 91:710-729, 1961. * Baxi, A.J., Balakrishnan, V., and Sanghvi, L.D. Deficiency of glucose-6-phosphate dehydrogenase-observations on a sample from Bombay. Curr.Sci. 30:16-17, 1961. * Bernasconi, C., Bedarida, G., Pollini, G., and Sartori, S. Studio del meccanismo di emolisi in un caso di anemia emolitica acquisita da piramidone. Haematol.Arch. 46:697-720, 1961. * Beutler, E. Sensitivity to hemolytic drugs: An inborn error of red blood cell metabolism. Am.J.Clin.Nutr. 9:700-704, 1961. Notes: (B70). * Bowman, J.E. and Walker, D.G. The origin of glucose-6-phosphate dehydrogenase deficiency in Iran: Theoretical considerations. Proc.2nd Int.Cong.Hum.Genet.:583-586, 1961. * Bowman, J.E. and Walker, D.G. Virtual absence of glutathione instability of the erythrocytes among Armenians in Iran. Nature 191:221-223, 1961. * Brewer, G.J. and Tarlov, A.R. Studies on the mechanism of primaquine-type hemolysis: The effect of methylene blue. Clin.Res. 9:65, 1961. * Brewer, G.J., Tarlov, A.R., and Kellermeyer, R.W. The hemolytic effect of primaquine. XII. Shortened erythrocyte life span in primaquine-sensitive male negroes in the absence of drug administration. J.Lab.Clin.Med. 58:217-224, 1961. * Budtz-Olsen, O. Absence of red cell enzyme deficiency in australian aborigines. Nature 192:765, 1961. * Charlton, R.W. and Bothwell, T.H. Primaquine-sensitivity of red cells in various races in Southern Africa. BMJ 1:941-944, 1961. * Cohen, G. and Hochstein, P. Glucose-6-phosphate dehydrogenase and detoxification of hydrogen peroxide in human erythrocytes. Science 134:1756-1757, 1961. * Danon, D., Sheba, C., and Ramot, B. The morphology of

glucose 6 phosphate dehydrogenase deficient erythrocytes: Electron-microscopic studies. Blood 17:229-234, 1961. * Doxiadis, S.A., Fessas, P., Valaes, T., and Mastrokalos, N. Glucose-6-phosphate dehydrogenase deficiency. Lancet 1:297-301, 1961. * Ells, H.A. and Kirkman, H.N. A colorimetric method for assay of erythrocytic glucose-6-phosphate dehydrogenase. Proc.Soc.Exp.Biol.Med. 106:607-609, 1961. * Fairbanks, V.F. and Beutler, E. A simple method for detection of erythrocyte glucose-6-phosphate dehydrogenase (G-6-PD) deficiency. Blood 18:783, 1961. Notes: (B69). * Furuhjelm, U. and Vuopio, P. Glucose-6-phosphate dehydrogenase deficiency. Lancet 2:1366, 1961. * Gant, F.L. and Winks, G.F.J. Primaquine sensitive hemolytic anemia complicating diabetic acidosis. Clin.Res. 9:27, 1961. * Gilles, H.M. and Taylor, B.G. The existence of the glucose-6-phosphate dehydrogenase deficiency trait in Nigeria and its clinical implications. Ann.Trop.Med.Parasitol. 55:64-70, 1961. * Harris, R. and Gilles, H.M. Glucose-6-phosphate dehydrogenase deficiency in the peoples of the Niger delta. Ann.Hum.Genet. 25:199-206, 1961. * Kellermeyer, R.W., Carson, P.E., Schrier, S.L., Tarlov, A.R., and Alving, A.S. The hemolytic effect of primaquine. XIV. Pentose metabolism in primaquine-sensitive erythrocytes. J.Lab.Clin.Med. 58:715-724, 1961. * Kidson, C. Deficiency of G 6 PD: Some aspects of the trait in people of Papua-New Guinea. Med.J.Aust. 48:506-509, 1961. * Kirkman, H.N. and Riley, H.D.J. Congenital nonspherocytic hemolytic anemia. Am.J.Dis.Child. 102:313-320, 1961. * Lhr, G.W. and Waller, H.D. Biochemie und pathogenese der enzymopenischen heemolytischen anemien. Dtsch.Med.Wochenschr. 86:27-38, 1961. * Marks, P.A., Szeinberg, A., and Banks, J. Erythrocyte glucose-6-phosphate dehydrogenase of normal and mutant human subjects: Properties of the purified enzyme. J.Biol.Chem. 236:10-17, 1961. * Motulsky, A.G. and Campbell-Kraut, J.M. Population genetics of glucose-6-phosphate dehydrogenase deficiency of the red cell. In: Proceedings of the Conference on Genetic Polymorphisms and Geographic Variations in Disease, edited by Blumberg, B.S.New York:Grune & Stratton, 1961,p. 159-180. * Motulsky, A.G. Glucose-6-phosphate dehydrogenase deficiency haemolytic disease of the newborn, and malaria. Lancet 1:1168-1169, 1961. * Pearson, H.A. and Druyan, R. Erythrocyte glucose-6-phosphate dehydrogenase activity related to thyroid activity. J.Lab.Clin.Med. 57:343-349, 1961. * Ramot, B., Ashkenazi, I., Rimon, A., Adam, A., and Sheba, C. Activation of glucose-6-phosphate dehydrogenase of enzyme-deficient subjects. II. Properties of the activator and the activation reaction. J.Clin.Invest. 40:611-616, 1961. * Robertson, D.H.H. Nitrofurazone-induced haemolytic anaemia in a refractory case of trypanosoma rhodesiense sleeping sickness: The haemolytic trait & self-limiting haemolytic anaemia. Ann.Trop.Med.Parasitol. 55:49-64, 1961. * Ryan, B.P.K. and Parsons, I.C. Glucose-6-phosphate dehydrogenase activity in anaemic papuans. Med.J.Aust. 2:502-506, 1961.

* Ryan, B.P.K. and Parsons, I.C. Glucose-6-phosphate dehydrogenase activity in Papuans. Nature 192:477, 1961. * Siniscalco, M., Bernini, L., Latte, B., and Motulsky, A.G. Favism and thalassaemia in Sardinia and their relationship to malaria. Nature 190:1179-1181, 1961. * Tada, K. Enzymatic anomaly of erythrocytes in congenital nonspherocytic hemolytic anemia. Tohoku J.Exp.Med. 75:263-267, 1961. * Tarlov, A. and Kellermeyer, R.W. The hemolytic effect of primaquine, XI. Decreased catalase activity in primaquine-sensitive erythrocytes. J.Lab.Clin.Med. 58:204-216, 1961. * Tarlov, A.R., Brewer, G.J., and Swanson, S.H. The effect of primaquine administration on the serum cholesterol of drug-sensitive American Negroes. Clin.Res. 9:190, 1961. * Trujillo, J., Fairbanks, V.F., Ohno, S., and Beutler, E. Chromosomal constitution in glucose-6-phosphate-dehydrogenase deficiency. Lancet 2:1454-1455, 1961. Notes: (B65). * Vella, F. The incidence of glucose-6-phosphate dehyrogenase deficiency in Singapore. Experientia 17:181-182, 1961. * Weed, R., Eber, J., and Rothstein, A. Effects of primaquine and other related compounds on the red blood cell membrane. I. Na+ and K+ permeability in normal human cells. J.Clin.Invest. 40:130-139, 1961. * Weed, R. Effects of primaquine on the red blood cell membrane. II. K+ permeability in glucose-6-phosphate dehydrogenase deficient erythrocytes. J.Clin.Invest. 40:140-143, 1961. * Wurzel, H., McCreary, T., Baker, L., and Gumerman, L. Glucose-6-phosphate dehydrogenase activity in platelets. Blood 17:314-318, 1961. * Zannos-Mariolea, L. and Kattamis, C. Glucose-6-phosphate dehydrogenase in Greece. Blood 18:34-47, 1961. * Zinkham, W.H. A deficiency of glucose-6-phosphate dehydrogenase activity in lens from individuals with primaquine-sensitive erythrocytes. Johns Hopkins Med.J. 109:206-216, 1961. * Adam, A., Sheba, C., Race, R.R., Sanger, R., Tippett, P., Hamper, J., and Gavin, J. Linkage relations of the X-borne genes responsible for glucose-6-phosphate dehydrogenase and for the Xg blood-groups. Lancet 1:1188-1189, 1962. * Bernard, J. and Dreyfus, J.C. Hemolyse aigue familiale et deficit de la glucose-6-phosphate desy- drogenase des erythrocytes. Nouv.Rev.Fr.Hematol. 2:135-138, 1962. * Bernstein, R.E. A rapid screening dye test for the detection of glucose-6-phosphate dehydrogenase deficiency in red cells. Nature 194:192-193, 1962. * Beutler, E. Biochemical abnormalities associated with hemolytic states. In: Mechanisms of Anemia in Man, edited by Weinstein, I.M. and Beutler, E.New York:McGraw-Hill, Inc. 1962,p. 195-236. Notes: (B72). * Beutler, E. Drug-induced haemolytic anaemias and the mechanism and significance of Heinz body formation in red blood cells. Nature 196:1095-1096, 1962. Notes: (B83). * Beutler, E. and Fairbanks, V.F. The normal human female as a mosaic of X-chromosome activity: Studies using glucose-6-phosphate dehydrogenase as a genetic marker. Proc.9th

Cong.Int.Soc.Hematol.Mexico City:43-53, 1962. Notes: (B92). * Beutler, E., Baluda, M.C., and Kelly, B.M. The role of methemoglobin in the mechanism of drug-induced hemolytic anemia. Proc.9th Cong.Int.Soc.Hematol.Mexico City:233-244, 1962. Notes: (B98). * Beutler, E., Yeh, M., and Fairbanks, V.F. The normal human female as a mosaic of X-chromosome activity: Studies using the gene for G-6-PD deficiency as a marker. Proc.Natl.Acad.Sci.USA 48:9-16, 1962. Notes: (B74). * Boyer, S.H., Porter, I.H., and Weilbacher, R.G. Electrophoretic heterogeneity of glucose-6-phosphate dehydrogenase and its relationship to enzyme deficiency in man. Proc.Natl.Acad.Sci.USA 48:1868-1876, 1962. * Brewer, G.J., Tarlov, A.R., Kellermeyer, R.W., and Alving, A.S. The hemolytic effect of primaquine. XV. Role of methemoglobin. J.Lab.Clin.Med. 59:905-917, 1962. * Brewer, G.J., Tarlov, A.R., and Alving, A.S. The methemoglobin reduction test for primaquine-type sensitivity of erythrocytes. JAMA 180:386-388, 1962. * Carson, P.E. and Tarlov, A.R. Biochemistry of hemolysis. Annu.Rev.Med. 13:105-126, 1962. * Choremis, C., Zannos-Mariolea, L., and Kattamis, M.D.C. Frequency of glucose-6-phosphate-dehydrogenase deficiency in certain highly malarious area of Greece. Lancet 1:17-18, 1962. * Erodohazi, M. and Highman, W.J. Glucose-6-phosphate-dehydrogenase deficiency in Britain. Lancet 2:1274, 1962. * Fairbanks, V.F. and Beutler, E. A simple method for detection of erythrocyte glucose-6-phosphate dehydrogenase deficiency (G-6-PD spot test). Blood 20:591-601, 1962. Notes: (B77). * Fessas, P., Doxiadis, S.A., and Valaes, T. Neonatal jaundice in glucose-6-phosphate dehydrogenase deficient infants. BMJ 2:1359-1362, 1962. * Gartler, S.M., Gandini, E., and Ceppellini, R. Glucose-6-phosphate dehydrogenase deficient mutant in human cell culture. Nature 193:602-603, 1962. * Gorman, J.G. and Kidson, C. Distribution pattern of an inherited trait, red cell enzyme deficiency, in New Guinea and New Britain. Am.J.Phys.Anthropol. 20:347-356, 1962. * Grumbach, M.M., Marks, P.A., and Morishima, A. Erythrocyte glucose-6-phosphate dehydrogenase activity and X-chromosome polysomy. Lancet 1:1330-1332, 1962. * Hailes, A.M. and Roberts, D.F. G 6 PD deficiency screening in Madeira. Hum.Biol. 34:206-213, 1962. * Harley, J.D. Acute haemolytic anaemia in Mediterranean children with glucose-6-phosphate dehydrogenase-deficient erythrocytes. Blood 19:257-258, 1962. * Kalmus, H. Distance and sequence of the loci for protan and deutan defects and for glucose-6-phosphate dehydrogenase deficiency. Nature 194:214-215, 1962. * Kidson, C. and Gorman, J.G. Contribution of red cell enzyme deficiency trait to an understanding of genetic relationships between Melanesian and other populations. Am.J.Phys.Anthropol. 20:357-363, 1962. * Kidson, C. and Gajdusek, D.C. Congenital defects of the central nervous system associated with hyperendemic goiter in a neolithic highland society of Netherlands New Guinea. II.

Glucose-6-phosphate dehydrogenase in the mulia population. Pediatrics 29:364-368, 1962. * Kidson, C. and Gorman, J.G. A challenge to the concept of selection by malaria in glucose-6-phosphate dehydrogenase deficiency. Nature 196:49-51, 1962. * Kidson, C. and Gajdusek, D.C. Glucose-6-phosphate dehydrogenase deficiency in Micronesian peoples. Aust.J.Sci. 25:61-62, 1962. * Kirkman, H.N. Glucose-6-phosphate dehydrogenase from human erythrocytes. I. Further purification and characterization. J.Biol.Chem. 237:2364-2370, 1962. * Kirkman, H.N. and Hendrickson, E.M. Glucose-6-phosphate dehydrogenase from human erythrocytes. II. Subactive states of the enzyme from normal persons. J.Biol.Chem. 237:2371-2376, 1962. * Kraus, A.P., Neely, C.L., Carey, F.T., and Kraus, L.M. Detection of deficient erythrocyte regeneration of reduced triphosphopyridine nucleotide from glucose-6-phosphate. Evaluation of a rapid screening test. Ann.Intern.Med. 56:765-773, 1962. * Kruatrachue, M., Choroenlarp, P., and Chongsuphajaisiddhi, T. Erythrocyte glucose-6-phosphate dehydrogenase and malaria in Thailand. Lancet 2:1183-1186, 1962. * Lisker, R., Loria, A., Llaven, J.G., Guttman, R., and Reyes, G.R. Note preliminaire sur la frequence des hemoglobulines anormales et de la deficience en G-6-PD dans la population Mexicaine. Rev.Franc.Etude Clin.Biol. 7:76-78, 1962. * Lhr, G.W. and Waller, H. Erythrozytenfermente. Z.Kinderheilkd. 159:120-137, 1962. * Marks, P.A., Banks, J., and Gross, R. Genetic heterogeneity of glucose-6-phosphate dehydrogenase deficiency. Nature 194:454-456, 1962. * Porter, I.H., Schulze, J., and McKusick, V.A. Genetical linkage between the loci for glucose-6-phosphate dehydrogenase deficiency and colour-blindness in American negroes. Ann.Hum.Genet. 26:107-122, 1962. * Sheba, C. and Adam, A. A survey of some genetical characters in Ethiopian tribes. Am.J.Phys.Anthropol. 20:167, 1962. * Szeinberg, A., Adam, A., and Sheba, C. The effect of in vitro incubation with nitrofurantoin on viability of normal and enzyme deficient red cells. Proc.Tel-hashomer Hospital 1:49-52, 1962. * Tarlov, A.R., Brewer, G.J., Carson, P.E., and Alving, A.S. Primaquine sensitivity. Glucose-6-phosphate dehydrogenase deficiency: An inborn error of metabolism of medical and biological significance. Arch.Intern.Med. 109:209-234, 1962. * Tnz, O. and Betke, K. Einfacher Farbtest zur Bestimmung der Glucose-6-phosphatdehydrogenase in menschlichen Erythrocyten. Klin.Wochenschr. 40:649-653, 1962. * Zail, S.S., Charlton, R.W., and Bothwell, T.H. The haemolytic effect of certain drugs in Bantu subjects with a deficiency of glucose-6-phosphate dehydrogenase. S.Afr.J.Med.Sci. 27:95-99, 1962. * Allison, A.C., Askonas, B.A., Barnicot, N.A., Blumberg, B.S., and Krimbas, C. Deficiency of erythrocyte glucose-6-phosphate dehydrogenase in Greek populations. Ann.Hum.Genet. 26:237-242, 1963. * Alvar-Loria, Q.B.P. Estudios sobre algunas caracteristacas hematologicas hereditarias en la poblacion Mexicana. III. Deficiencia en la glucosa 6-fosfato deshidrogenasa eritrocitica en 7 grupos indigenas y algunos mestizos. Gac.Med.Mex.

93:299-303, 1963. * Balinsky, D. and Bernstein, R.E. The purification and properties of glucose-6-phosphate dehydrogenase from human erythrocytes. Biochim.Biophys.Acta 67:313-315, 1963. * Balinsky, D. and Bernstein, R.E. Oxidation of reduced glutathione by acetylphenylhydrazine. Nature 199:187-188, 1963. * Baxi, A.J., Balakrishnan, V., Undevia, J.V., and Sanghvi, L.D. Glucose-6-phosphate dehydrogenase deficiency in the Parsee community, Bombay. Indian J.Med.Sci. 17:493-500, 1963. * Bernstein, R.E. Occurrence and clinical implications of red-cell glucose-6-phosphate dehydrogenase deficiency in South African racial groups. S.Afr.Med.J. 37:447-451, 1963. * Bernstein, R.E. Brilliant cresyl blue screening test for demonstrating glucose-6-phosphate dehydrogenase deficiency in red cells. Clin.Chim.Acta 8:158-160, 1963. * Beutler, E., Dern, R.J., and Baluda, M.C. A new technique for the ascertainment of heterozygotes for G-6-PD deficiency. In: Proc. 9th Cong. Europ. Soc. Haematol.Anonymous Lisbon:S. Karger, 1963,p. 675-684. Notes: (B108). * Capps, F.P.A., Gilles, H.M., Jolly, H., and Worlledge, S.M. Glucose-6-phoshate dehydrogenase deficiency and neonatal jaundice in Nigeria. Their relation to use of prophylactic vitamin K. Lancet 2:379-383, 1963. * Caruso, P., Conti, F., and Londrillo, A. Diagramma delle attivita enzimatiche endoeritrocitarie nel neonato, nel lattante, nel bambino. Minerva Pediatr. XX:1136-1145, 1963. * Chatterji, S.C. and Das, P.K. Chloramphenicol induced haemolytic anaemia due to enzymatic deficiency of erythrocytes. J.Indian Med.Assoc. 40:172-174, 1963. * Choremis, C., Kattamis, C., Zannos-Mariolea, L., Fessas, P., Stamatoyannopoulos, G., Karaklis, A., and Belios, G. Three inherited red-cell abnormalities in a district of Greece. Lancet 1:907-909, 1963. * Chung, A.E. and Langdon, R.G. Human erythrocyte glucose 6-phosphate dehydrogenase. II. Enzyme-coenzyme interrelationship. J.Biol.Chem. 238:2317-2324, 1963. * Chung, A.E. and Langdon, R.G. Human erythrocyte glucose-6-phosphate dehydrogenase I. Isolation and properties of the enzyme. J.Biol.Chem. 238:2309-2316, 1963. * Davidson, R.G., Migeon, B.R., Borden, M., and Childs, B. Dosage compensation in the regulation of erythrocyte glucose-6-phosphate dehydrogenase activity. Johns Hopkins Med.J. 112:318-322, 1963. * Davidson, R.G., Nitowsky, H.M., and Childs, B. Demonstration of two populations of cells in the human female heterozygous for glucose-6-phosphate dehydrogenase variants. Proc.Natl.Acad.Sci.USA 50:481-485, 1963. * Dern, R.J., Glynn, M.F., and Brewer, G.J. Studies on the correlation of the genetically determined trait, glucose-6-phosphate dehydrogenase deficiency, with behavioral manifestations in schizophrenia. J.Lab.Clin.Med. 62:319-329, 1963. * Fischler, E. and Wallis, K. Investigation of drug sensitivity in Shigella and its correlation with in vivo sensitivity. Ann.Paediat. 201:49-63, 1963. * Jaffe, E.R. The reduction of methemoglobin in erythrocytes of a patient with congenital methemoglobinemia, subjects with erythrocyte glucose-6-phosphate dehydrogenase deficiency, and normal individuals. Blood 21:561-572, 1963.

* Jim, R.T.S. and Chu, F.K. Hyperbilirubinemia due to glucose-6-phosphate dehydrogenase deficiency in a newborn Chinese infant. Pediatrics 31:1046-1049, 1963. * Kirkman, H. and Crowell, B.B. Molecular deficiency of glucose-6-phosphate dehydrogenase in primaquine sensitivity. Nature 197:286-287, 1963. * Kirkman, H.N. Genetic control of human enzymes. Pediatr.Clin.North Am. 10:299-318, 1963. * Kirkman, H.N. and Hendrickson, E.M. Sex-linked electrophoretic difference in glucose-6-phosphate dehydrogenase. Am.J.Hum.Genet. 15:241-258, 1963. * Lee, T.C., Shih, L.Y., Huang, P.C., Lin, C.C., Blackwell, B.N., Blackwell, R.Q., and Hsia, D.Y. Glucose-6-phosphate dehydrogenase deficiency in Taiwan. Am.J.Hum.Genet. 15:126-132, 1963. * Lewis, R.A. and Hathorn, M. Glucose-6-phosphate dehydrogenase deficiency correlated with S. hemoglobin. Ghana Med.J. 2:131-XXX, 1963. * Marks, P. G6PD deficiency in different population groups. In: The Genetics of Migrant and Isolate Populations, edited by Goldschmidt, E.Baltimore:Williams and Wilkins, 1963,p. 75-82. * Marks, P.A. and Tsutsui, E.A. Human glucose-6-P dehydrogenase: Studies on the relation between antigenicity and catalytic activity -- the role of TPN. Ann.NY Acad.Sci. 103:903-914, 1963. * Neimann, N., Dreyfus, J.C., Pierson, M., Ducas, J., and Stoessel, J.M. Le methemoglobinemie congenitale et recessive. Son association avec le deficit en glucose 6 phosphate deshydrogenase et la thalassemie mineure. Rev.Franc.Etude Clin.Biol. 8:757-764, 1963. * O'Flynn, M.E.D. and Hsia, D.Y. Serum bilirubin levels and glucose-6-phosphate dehydrogenase deficiency in newborn American negroes. J.Pediatr. 63:160-161, 1963. * Oski, F.A., Shahidi, N.T., and Diamond, L.K. Erythrocyte acid phosphomonesterase and glucose-6-phosphate dehydrogenase deficiency in caucasians. Science 139:409-410, 1963. * Pinkhas, J., Djaldetti, M., Joshua, H., Resnick, C., and De Vries, A. Sulfhemoglobinemia and acute hemolytic anemia with Heinz bodies following contact with a fungicide-zinc ethylene bisidithiocarbamate in subject with glucose-6-phosphate dehydrogenase deficiency and hypocatalasemia. Blood 21:484-494, 1963. * Piomelli, S., Puca, F., and Siniscalco, M. Possibili variazioni individuali nellassorbimento del principio attivo delle fave in rapporto al favismo clinico. Atti Ass.Genet.It. 8:100, 1963. * Prins, H.K., Loos, J.A., and Meuwissen, J.H.E. G 6 PD deficiency in West New Guinea. Trop.Geogr.Med. 15:361-370, 1963. * Salvidio, E., Pannacciulli, I., and Tizianello, A. G-6-PD deficient states in Sardinians. In: Proc. 9th Cong. Europ. Soc. Haematol.Anonymous Lisbon:S. Karger, 1963,p. 707-714. * Sansone, G., Rovei, S., and Rasore-Quartino, A. Anemia emolitica acuta associata ad epatite virale in un bambino con deficienza in glucosio-6-fosfato deidrogenasi eritrocitaria. Giornale de Malattie Infettive 8:1-7, 1963. * Sass, M.D., Vorsanger, E., and Spear, P.W. Enzyme activity as an indicator of red cell age. Clin.Chim.Acta 10:21-26, 1963. * Schaerer, K., Herzka, H., and Marti, H.R. Kernicterus bei Mangel an Glukose-6-phosphat-Dehydrogenase der Erythrocyten. Helv.Paediatr.Acta 2:148-162, 1963.

* Sutton, R.N.P. Erythrocyte glucose-6-phosphate-dehydrogenase deficiency in Trinidad. Lancet 1:855, 1963. * Szeinberg, A. G6PD deficiency among Jews--genetic and anthropological considerations. In: The Genetics of Migrant and Isolate Populations, edited by Goldschmidt, E.Philadelphia:Williams and Wilkins, 1963,p. 69-72. * Szeinberg, A., Oliver, M., Schmidt, R., Adam, A., and Sheba, C. Glucose-6-phosphate dehydrogenase deficiency and haemolytic disease. Arch.Dis.Child. 38:23-28, 1963. * Tizianello, A., Pannacciulli, I., Salvidio, E., and Gay, A. Erythrocytic glucose-6-phosphate dehydrogenase deficiency as a problem in the selection of blood donors. Vox Sang. 8:47-50, 1963. * Valaes, T., Doxiadis, S., and Fessas, P. Acute hemolysis due to naphthalene inhalation. J.Pediatr. 63:904-915, 1963. * Zinkham, W.H. Peripheral blood and bilirubin values in normal full-term primaquine-sensitive negro infants: Effect of vitamin K. Pediatrics 31:983-995, 1963. * Ben-Ishay, D. and Izak, G. Chronic hemolysis associated with glucose-6-phosphate deficiency. J.Lab.Clin.Med. 63:1002-1009, 1964. * Bernini, L., Latte, B., Siniscalco, M., Piomelli, S., Spada, U., Adinolfi, M., and Mollison, P.L. Survival of 51 Cr-labelled red cells in subjects with thalassemia-trait or G6PD deficiency or both abnormalities. Br.J.Haematol. 10:171-180, 1964. * Beutler, E. and Baluda, M.C. The separation of glucose-6-phosphate dehydrogenase-deficient erythrocytes from the blood of heterozygotes for glucose-6-phosphate dehydrogenase deficiency. Lancet 1:189-192, 1964. Notes: (B99). * Beutler, E. The distribution of gene products among populations of cells in heterozygous humans. Cold Spring Harbor Symp.Quant.Biol. 29:261-271, 1964. Notes: (B112). * Beutler, E. and Sparkes, R.S. Variation of glucose-6-phosphate dehydrogenase in different populations. Lancet 2:95, 1964. Notes: (B109). * Beutler, E. and Baluda, M.C. Isolation of enzyme-deficient erythrocytes from blood of G 6 PD deficient heterozygotes. Clin.Res. 12:220, 1964. Notes: (B103). * Beutler, E. Drug-induced blood dyscrasias. III. Hemolytic anemia. JAMA 189:143-144, 1964. Notes: (B104). * Bonsignore, A., Foranini, A., Fantoni, A., Leoncini, G., and Segni, P. Relationship between age and enzymatic activities in human erythrocytes from normal and fava-bean-sensitive subjects. J.Clin.Invest. 43:834-842, 1964. * Brewer, G., Powell, R.D., Tarlov, A.R., and Alving, A.S. Hemolytic effect of primaquine. XVI. Glyoxalase activity of primaquine-sensitive and normal erythrocytes. J.Lab.Clin.Med. 63:106-121, 1964. * Brewer, G.J., Powell, R.D., Swanson, S.H., and Alving, A.S. Hemolytic effect of primaquine. XVII. Hexokinase activity of glucose-6-phosphate dehydrogenase-deficient and normal erythrocytes. J.Lab.Clin.Med. 64:601-612, 1964. * Chan, T.K., Todd, D., and Wong, C.C. Erythrocyte glucose-6-phosphate dehydrogenase deficiency in Chinese. BMJ 2:102, 1964.

* Chanmugam, D. and Frumin, A.M. Abnormal oral glucose tolerance response in erythrocyte glucose-6-phosphate dehydrogenase deficiency. N.Engl.J.Med. 271:1202-1204, 1964. * Cohen, G. and Hochstein, P. Generation of hydrogen peroxide in erythrocytes by hemolytic agents. Biochemistry 3:895-900, 1964. * Doxiadis, S.A. and Valaes, T. The clinical picture of glucose 6-phosphate dehydrogenase deficiency in early infancy. Arch.Dis.Child. 39:545-553, 1964. * Dreyfus, J.C., Maleknia, N., and Kaplan, J.C. Recherches sur le deficit en glucose-6-phosphate deshydrogenase en France. A propos de 200 dosages. Nouv.Rev.Fr.Hematol. 4:791-802, 1964. * Eng, L.L. and Giok, P.H. Glucose-6-phosphate dehydrogenase deficiency in Indonesia. Nature 204:88-89, 1964. * Eng, L.L. and Ti, T.S. Glucose-6-phosphate dehydrogenase deficiency in Malayans. Trans.R.Soc.Trop.Med.Hyg. 58:500-502, 1964. * Eng, L.L., Chin, J., and Ti, T.S. Glucose-6-phosphate dehydrogenase deficiency in Brunei, Sabah and Sarawak. Ann.Hum.Genet. 28:173-176, 1964. * Eng, L.L. and Chin, J. Abnormal haemoglobin and glucose-6-phosphate dehydrogenase deficiency in Malayan aborigines. Nature 204:291-292, 1964. * Escobar, M.A., Heller, P., and Trobaugh, F.E.J. "Complete" erythrocyte glucose-6-phosphate dehydrogenase deficiency. Arch.Intern.Med. 113:428-434, 1964. * Flatz, G. and Sringam, S. Glucose-6-phosphate dehydrogenase deficiency in different ethnic groups in Thailand. Ann.Hum.Genet. 27:315-318, 1964. * Flatz, G., Thanangkul, O., Simarak, S., and Manmontri, M. Glucose-6-phosphate dehydrogenase deficiency and jaundice in newborn infants in Northern Thailand. Ann.Paediat. 203:39-45, 1964. * Fornaini, G., Bianchini, E., Leoncini, G., and Fantoni, A. Metabolic aspects of red cells in congenital non-spherocytic haemolytic anaemia. Br.J.Haematol. 10:23-35, 1964. * Fraser, G.R., Defaranas, B., Kattamis, C.A., Race, R.R., Sanger, R., and Stamatoyannopoulos, G. Glucose-6-phosphate dehydrogenase, colour vision and Xg blood groups in Greece: Linkage and population data. Ann.Hum.Genet. 27:395-403, 1964. * Gabor, E.P., Lowenstein, L., and De Leeuw, N.K. Hemolytic anemia induced by phenylazo-diamino-pyridine (Pyridium). Can.Med.Assoc.J. 91:756-759, 1964. * Gartler, S.M. and Linder, D. Developmental and evolutionary implications of the mosaic nature of the G-6-PD system. Cold Spring Harbor Symp.Quant.Biol. 29:253-260, 1964. * Hayes, D.M. and Felts, J.H. Sulfonamide methemoglobinemia and hemolytic anemia during renal failure. Am.J.Med.Sci. 247:552-557, 1964. * Jeannet, M., Perrier, C.V., and Tnz, O. Anemie hemolytique aigue par la nitrofurantoine chez une Iranienne presentant un deficit en glucose-6-phosphate dehydrogenase erythrocytaire. Schweiz.Med.Wochenschr. 94:939-943, 1964. * Kahn, P.M. Glucose-6-phosphate dehydrogenase deficiency in an Indian rural area. Genetics 59:14-18, 1964. * Kirkman, H.N., Rosenthal, I.M., Simon, E.R., Carson, P.E., and Brinson, A.G. "Chicago I" variant of glucose-6-phosphate dehydrogenase in congenital hemolytic disease. J.Lab.Clin.Med. 63:715-725, 1964. * Kirkman, H.N., Schettini, F., and Pickard, B.M.

Mediterranean variant of glucose-6-phosphate dehydrogenase. J.Lab.Clin.Med. 63:726-735, 1964. * Kirkman, H.N., McCurdy, P.R., and Naiman, J.L. Functionally abnormal glucose-6-phosphate dehydrogenases. Cold Spring Harbor Symp.Quant.Biol. 29:391-398, 1964. * Levin, S.E., Charlton, R.W., and Freiman, I. Glucose-6-phosphate dehydrogenase deficiency and neonatal jaundice in South African Bantu infants. J.Pediatr. 65:757-764, 1964. * Linhard, J., Baylet, R., and Malvoisin, J. Premiers resultats sur les deficiences en G 6 PD dans la region de dakar. Bul.Soc.Med.Afr.Noire Land.Fr. 9:269-270, 1964. * Mager, J., Razin, A., Hershko, A., and Izak, G. The mechanism of red-cell hexokinase inhibition induced by oxidation of intracellular glutathione and its relation to drug sensitivity. Biochem.Biophys.Res.Commun. 17:703-708, 1964. * Mohler, D.N. and Crockett, C.L.J. Hereditary hemolytic disease secondary to glucose-6-phosphate dehydrogenase deficiency: Report of three cases with special emphasis on ATP metabolism. Blood 23:427-444, 1964. * Motulsky, A.G., Stransky, E., and Fraser, G.R. Glucose-6-phosphate dehydrogenase (G6PD) deficiency, thalassaemia, and abnormal haemoglobins in the Philippines. J.Med.Genet. 1:102-106, 1964. * Nance, W.E. Turner's syndrome, twinning, and an unusual variant of glucose-6-phosphate dehydrogenase. Am.J.Hum.Genet. 16:380-392, 1964. * Nance, W.E. Genetic tests with a sex-linked marker: G-6-PD. Cold Spring Harbor Symp.Quant.Biol. 29:415-425, 1964. * Oezer, L. and Mills, G.C. Elliptocytosis with haemolytic anemia. Br.J.Haematol. 10:468-476, 1964. * Papayannopoulou, T. and Stamatoyannopoulos, G. Pseudo-mosaicism in males with mild glucose-6-phosphate dehydrogenase deficiency. Lancet 2:1215-1217, 1964. * Plato, C.C., Cruz, M.T., and Kurland, L.T. Frequency of glucose-6-phosphate dehydrogenase deficiency, red-green colour blindness and Xga blood-group among chamorros. Nature 202:728, 1964. * Plato, C.C., Rucknagel, D.L., and Gershowitz, H. Studies on the distribution of glucose-6-phosphate dehydrogenase deficiency, thalassemia, and other genetic traits in the coastal and mountain villages of Cyprus. Am.J.Hum.Genet. 16:267-283, 1964. * Porter, I.H., Boyer, S.H., Watson-Williams, E.J., Adam, A., Szeinberg, A., and Siniscalco, M. Variation of glucose-6-phosphate dehydrogenase in different populations. Lancet 1:895-899, 1964. * Rakitzis, E.T. Test for glucose-6-phosphate dehydrogenase deficiency. Lancet 2:1182-1183, 1964. * Ramot, B., Bauminger, S., Brok, F., Gafni, D., and Shwartz, J. Characterization of glucose-6-phosphate dehydrogenase in Jewish mutants. J.Lab.Clin.Med. 64:895-904, 1964. * Ramot, B. and Brok, F. A new glucose-6-phosphate dehydrogenase mutant (Tel-Hashomer mutant). Ann.Hum.Genet. 28:167-172, 1964. * Sansone, G., Rasore-Quartino, A., and Veneziano, G. Two red-cell populations in the human female heterozygous for G-6-PD deficiency. Lancet 1:329, 1964. * Shows, T.B., Tashian, R.E., and Brewer, G.J. Erythrocyte glucose-6-phosphate dehydrogenase in caucasians: New inherited variant. Science 145:1056-1057, 1964.

* Siniscalco, M. and Filippi, G. Recombination between protan and deutan genes; data on their relative positions in respect of the G6PD locus. Nature 204:1062-1064, 1964. * Srivastava, S.K., Zaheer, N., and Krishnan, P.S. Specific inhibition of hepatic glucose-6-phosphate dehydrogenase in iron deficiency anemia in albino rats. Arch.Biochem.Biophys. 105:446-447, 1964. * Stamatoyannopoulos, G. and Fessas, P. Thalassemia, glucose-6-phosphate dehydrogenase deficiency, sickling and malarial endemicity in Greece: A study of five areas. BMJ 1:875-879, 1964. * Szeinberg, A. and Clejan, L. Sulfhydryl groups in the red cells of normal and glucose-6-phosphate dehydrogenase-deficient subjects. Biochim.Biophys.Acta 93:564-572, 1964. * Taleb, N., Loiselet, J., Ghorra, F., and Sfeir, H. Sur la deficience en glucose-6-phosphate-deshydrogenase dans les populations autochtones du Liban. C.R.Acad.Sci.(Paris) 258:5749-5751, 1964. * Tnz, O. and Rossi, E. Morphological demonstration of two red cell populations in human females heterozygous for glucose-6-phosphate dehydrogenase deficiency. Nature 202:606-607, 1964. * Van der Sar, A., Schouten, H., and Struyker Boudier, A.M. Glucose-6-phosphate dehydrogenase deficiency in red cells. Incidence in the Curacao population, its clinical and genetic aspects. Enzyme 27:289-310, 1964. * Young, W.J., Porter, J.E., and Childs, B. Glucose-6-phosphate dehydrogenase in drosophila: X-linked electrophoretic variants. Science 143:140-141, 1964. * Andre, R., Dreyfus, B., Malassenet, R., and Sultan, C. Deux observations d'anemie hemolytique aigue apres prise de phenyl-semi-carbazide. Nouv.Rev.Fr.Hematol. 5:431-444, 1965. * Beaconsfield, P., Rainsbury, R., and Kalton, G. Glucose-6-phosphate dehydrogenase deficiency and the incidence of cancer. Oncology 19:11-19, 1965. * Belton, E.M. and Jones, R.V. Haemolytic anaemia due to nalidixic acid. Lancet 2:691, 1965. * Berry, D.H. and Vietti, T.J. Clinical manifestations of primaquine-sensitive anemia. Am.J.Dis.Child. 110:166-171, 1965. * Beutler, E. and Baluda, M.C. The separation of glucose-6-phosphate dehydrogenase deficient erythrocytes from blood of heterozygotes for glucose-6-phosphate dehydrogenase deficiency. Folia Haematol.(Leipz.) 83:410-415, 1965. Notes: (B123). * Beutler, E. and Collins, Z. Hybridization of glucose-6-phosphate dehydrogenase from rat and human erythrocytes. Science 150:1306-1307, 1965. Notes: (B130). * Beutler, E. Glucose-6-phosphate dehydrogenase deficiency. In: The Metabolic Basis of Inherited Disease, edited by Stanbury, J.B., Wyngaarden, J.B., and Fredrickson, D.S.New York:McGraw-Hill, Inc. 1965,p. 1060-1089. Notes: (B134). * Beutler, E. Drug-induced blood dyscrasias. III. Hemolytic anemia. J.Oral Ther.Pharmacol. 1:567-568, 1965. Notes: (B118). * Beutler, E. and Collins, Z. Pseudo-mosaicism in males with mild glucose-6-phosphate dehydrogenase deficiency. Lancet 1:552-553, 1965. Notes: (B114).

* Beutler, E. Glucose-6-phosphate dehydrogenase deficiency and non-spherocytic congenital hemolytic anemia. Semin.Hematol. 2:91-138, 1965. Notes: (B117). * Beutler, E. New screening methods for pyruvate kinase (PK) deficiency, G-6-PD deficiency, GSSG-R deficiency, and galactosemia. Clin.Res. 13:546, 1965. Notes: (B122A). * Bowman, J.E., Brewer, G.J., Frischer, H., Carter, J.L., Eisenstein, R.B., and Bayrakci, C. A re-evaluation of the relationship between glucose-6-phosphate dehydrogenase deficiency and the behavioral manifestations of schizophrenia. J.Lab.Clin.Med. 65:222-227, 1965. * Boyer, S.H. and Graham, J.B. Linkage between the X chromosome loci for glucose-6-phosphate dehydrogenase electrophoretic variation and hemophilia A. Am.J.Hum.Genet. 17:320-324, 1965. * Brewer, G.J., Gall, J.C., Honeyman, M.S., Gershowitz, M., Dern, R.J., and Hames, O. Inheritance of quantitative expression of G 6 PD deficiency in heterozygous negro females. Clin.Res. 13:265, 1965. * Brown, W.R. and Boon, W.H. Ethnic group differences in plasma bilirubin levels of full-term, healthy Singapore newborns. Pediatrics 36:745-751, 1965. * Brunetti, P. Incidenca del difetto di G-6-PD nell' italia centrale. Haematologica (Pavia) 50:203-219, 1965. * Chan, T.K., Todd, D., and Wong, C.C. Tissue enzyme levels in erythrocyte glucose-6-phosphate dehydrogenase deficiency. J.Lab.Clin.Med. 66:937-941, 1965. * Dodin, A. Deficit en glucose 6 phosphate deshydrogenase. Arch.Inst.Pasteur Madagascar 33:233-237, 1965. * Ezra, R., Szeinberg, A., and Sheba, C. Catalase activity in normal and glucose-6-phosphate dehydrogenase deficient red cells. Isr.J.Med.Sci. 1:847-849, 1965. * Freier, S., Mayer, K., Abrahamov, A., and Levene, C. Neonatal jaundice in infants with enzymatic defect of the red blood cell. Isr.J.Med.Sci. 1:844-847, 1965. * Gall, J.C.J., Brewer, G.J., and Dern, R.J. Studies of glucose-6-phosphate dehydrogenase activity of individual erythrocytes: The methemoglobin-elution test for identification of females heterozygous for G6PD deficiency. Am.J.Hum.Genet. 17:359-368, 1965. * Ganzoni, A. and Rhomberg, F. Hemolytic crisis in glucose-6-phosphate dehydrogenase deficiency and lead poisoning. Acta Haematol.(Basel) 34:338-346, 1965. * Gelpi, A.P. Glucose-6-phosphate dehydrogenase deficiency in Saudi Arabia: A survey. Blood 25:486-493, 1965. * Greenberg, L.H. and Tanaka, K.R. Hereditary hemolytic anemia due to glucose-6-phosphate dehydrogenase deficiency. Am.J.Dis.Child. 110:206-209, 1965. * Hendrickse, R.G. In discussion of paper by Motulsky, A. Theoretical and clinical problems of glucose-6-phosphate dehydrogenase deficiency. Its occurrence in Africans and its combination with hemoglobinopathy. In: A symposium, edited by Jonxis, J.H.P.Oxford:Blackwell, 1965,p. 208 * Hoskova, A., Cech, M., and Noll, A. O moznosti defektu glukozo-6-fosfatdehydrogenazy u nas. Cas.Lek.Cesk. 104:262, 1965. * Kaplan, J.C., Dreyfus, J.C., and Bessis, M. La structure en mosaique du chromosome x chez la femme. Nouv.Rev.Fr.Hematol. 5:835-850, 1965.

* Kirimlidis, S., Politis, E., Drossos, C., Scaloumbakas, N., Papaioannou, M., and Phillippidis, P. Glucose-6-phosphate-dehydrogenase deficiency in Greece. Study by using a modification of Beutler and Fairbanks spot test. Helv.Paediatr.Acta 20:490-496, 1965. * Kirkman, H.N., Doxiadis, S.A., Valaes, T., Tassopoulos, N., and Brinson, A.G. Diverse characteristics of glucose-6-phosphate dehydrogenase from Greek children. J.Lab.Clin.Med. 65:212-221, 1965. * Kirkman, H.N., Simon, E.R., and Pickard, B.M. Seattle variant of glucose-6-phosphate dehydrogenase. J.Lab.Clin.Med. 66:834-840, 1965. * Knox, E.G. and McGregor, I.A. G 6 PD deficiency in a Gambian village. Trans.R.Soc.Trop.Med.Hyg. 59:46-58, 1965. * Lewis, R.A. and Hathorn, M. Correlation of S hemoglobin with glucose-6-phosphate dehydrogenase deficiency and its significance. Blood 26:176-180, 1965. * Linder, D. and Gartler, S.M. Glucose-6-phosphate dehydrogenase mosaicism: Utilization as cell marker in the study of leiomyomas. Science 150:67-69, 1965. * Lisker, R., Loria, A., and Cordova, M.S. Studies on several genetic hematological traits of the Mexican population. VIII. Hemoglobin S, glucose-6-phosphate dehydrogenase deficiency, and other characteristics in a malarial region. Am.J.Hum.Genet. 17:179-187, 1965. * Lisker, R. Caracteristicas geneticas hematologicas de la poblacion Mexicana. Gac.Med.Mex. 95:1027-1036, 1965. * Long, W.K., Kirkman, H.N., and Sutton, H.E. Electrophoretically slow variants of glucose-6-phosphate dehydrogenase from red cells of negroes. J.Lab.Clin.Med. 65:81-87, 1965. * Luttrell, V. and Lea, C. G 6 PD deficiency in Africans. East Afr.Med.J. 42:313-315, 1965. * Luzzatto, L. and Allan, N.C. Different properties of glucose-6-phosphate dehydrogenase from human erythrocytes with normal and abnormal enzyme levels. Biochem.Biophys.Res.Commun. 21:547-554, 1965. * Marti, H.R., Schoepf, K., and Gsell, O.R. Frequency of haemoglobin S and G-6-PD deficiency in Southern tanzania. BMJ 1:1476, 1965. * Mathai, C., Trujillo, J., Ohno, S., and Beutler, E. Sex-linkage of G-6-PD in the horse and donkey. Fed.Proc. 24:440, 1965. Notes: (B140). * Miwa, S., Momma, K., Komiya, K., Ise, T., Irisawa, K., and Oyama, H. Glucose-6-phosphate dehydrogenase (G-6-PD) deficiency. I. Report of a case found in Japanese, with special reference to the enzyme activation by stroma of normal erythrocytes. Acta Haematol.Jpn. 28:585-589, 1965. * Miwa, S., Teramura, K., Irisawa, K., and Oyama, H. Glucose-6-phosphate dehyrogenase (G-6-PD) deficiency. II. Incidence of G-6-PD deficiency in Japanese. Acta Haematol.Jpn. 28:590-592, 1965. * Modiano, G., Benerecetti-Santachiara, A.S., Gonano, F., Zei, G., Capaldo, A., and Cavalli-Sforza, L.L. An analysis of ABO, MN, RH, HP, TF and G-6-PD types in a sample from the human population of the Lecce province. Ann.Hum.Genet. 29:19-31, 1965. * Motulsky, A.G., Lee, T.C., and Fraser, G.R. Glucose-6-phosphate dehydrogenase (G6PD) deficiency, thalassaemia, and abnormal haemoglobins in Taiwan. J.Med.Genet.

2:18-20, 1965. * Nitowsky, H.M., Soderman, D.D., and Herz, F. Glucose-6-phosphate-dehydrogenase deficiency in Filipinos. Lancet 1:917, 1965. * Obbink, H.J.K. Glucose-6-phosphate dehydrogenase deficiency in a dutch family. Acta Genet. 15:21-32, 1965. * Ohno, S., Poole, J., and Gustavsson, I. Sex-linkage of erythrocyte glucose-6-phosphate dehydrogenase in two species of wild hares. Science 150:1737-1738, 1965. * Oski, F.A. and Growney, P.M. A simple micromethod for the detection of erythrocyte glucose-6-phosphate dehydrogenase deficiency. J.Pediatr. 66:90-93, 1965. * Pannacciulli, I., Tizianello, A., Ajmar, F., and Salvidio, E. The course of experimentally-induced hemolytic anemia in a primaquine- sensitive caucasian. A case study. Blood 25:92-95, 1965. * Ruffie, J. and Taleb, N. In: Etude Hemotypologique des Ethnies Libanaises,Anonymous Paris:Hermann, 1965, * Say, B., Ozand, P., Berkel, I., and Cevik, N. Erythrocyte glucose-6-phosphate dehydrogenase deficiency in Turkey. Acta Paediatr.Scand. 54:319-324, 1965. * Schettini, F., Meloni, T., Mela, C., and Fanciulli, G. Red cell acid phosphatase in normal and glucose-6-phosphate dehydrogenase deficiency Sardinian subjects. Acta Haematol.(Basel) 33:230-236, 1965. * Shafer, A.W. The carbohydrate intermediates of erythrocytes deficient in glucose-6-phosphate dehydrogenase. Blood 26:82-90, 1965. * Shaw, C.R. and Barto, E. Autosomally determined polymorphism of glucose-6-phosphate dehydrogenase in peromyscus. Science 148:1099-1100, 1965. * Sklavunu-Zurukzoglu, S., Mameletzis, C., and Katriu, D. Observations on the glucose-6-phosphate dehydrogenase of the breast milk. Helv.Paediatr.Acta 20:193-196, 1965. * Smink, D.A. and Prins, H.K. Hereditary and acquired blood factors in the negroid population of Surinam. V. Electrophoretic heterogeneity of G-6-PD. Trop.Geogr.Med. 17:236-242, 1965. * Srivastava, S.K., Sanwal, G.G., and Tewari, K.K. Biochemical alterations in rat tissue in iron deficiency anaemia and repletion with iron. Indian J.Biochem.Biophys. 2:257-266, 1965. * Szeinberg, A., Zaidman, J., and Clejan, L. Investigation of the lipid content of normal and glucose-6-phosphate dehydrogenase deficient red cells. Biochim.Biophys.Acta 98:598-606, 1965. * Szeinberg, A., Zaidman, J., and Clejan, L. Investigation of the lipid content of normal and glucose-6-phosphate dehydrogenase deficient red cells. Isr.J.Med.Sci. 1:833-835, 1965. * Tnz, O. The problem of defining the heterozygous carrier in glucose-6-phosphate dehydrogenase deficiency. Ann.Paediat. 204:24-41, 1965. * Walter, H., Neumann, S., and Nemeskeri, J. Populationgenetische Untersuchungen ber die Verteilung von Haemoglobin S und glucose-6-phosphat-dehydrogenasemangel im Bodrogkoez (Nordostungarn). Humangenetik 1:651-657, 1965. * Wong, P.W.K., Shih, L.-.Y., and Hsia, D.Y.Y. Characterization of glucose-6-phosphate dehydrogenase among Chinese. Nature 208:1323-1324, 1965. * Yue, P.C.K. and Strickland, M. Glucose-6-phosphate-dehydrogenase deficiency and neonatal jaundice in Chinese male infants in Hong Kong. Lancet 1:350-351, 1965.

* Adam, A., Sheba, C., Sanger, R., and Race, R.R. The linkage relation of G6PD to Xg. Am.J.Hum.Genet. 18:110, 1966. * Avigad, G. Inhibition of glucose-6-phosphate dehydrogenase by adenosine-5-triphosphate. Proc.Natl.Acad.Sci.USA 56:1543-1547, 1966. * Beutler, E. Pathogenesis and diagnosis of spontaneous and drug-induced hemolytic anemia due to lack of G-6-PD in the erythrocyte. In: Relazione al VI Congresso Internationale di Patologia Clinica,Anonymous Rome:Edizioni C.E.P.I. 1966,p. 297-305. Notes: (B153). * Beutler, E. A series of new screening procedures for pyruvate kinase deficiency, glucose-6-phosphate dehydrogenase deficiency, and glutathione reductase deficiency. Blood 28:553-562, 1966. Notes: (B154). * Beutler, E. and Collins, Z. Hybridization studies in the further characterization of erythrocyte glucose-6-phosphate dehydrogenase. Experientia 22:827-828, 1966. Notes: (B165). * Bishop, C. Assay of glucose-6-phosphate dehydrogenase (E.C. 1.1.1.49) And 6-phosphogluconate dehydrogenase (E.C. 1.1.1.43) In red cells. J.Lab.Clin.Med. 68:149-155, 1966. * Bonsignore, A., Fornaini, G., Leoncini, G., Fantoni, A., and Segni, P. Characterization of leukocyte glucose 6-phosphate dehydrogenase in Sardinian mutants. J.Clin.Invest. 45:1865-1874, 1966. * Boon, W.H. Viral hepatitis in G-6-PD deficiency. Lancet 1:882-883, 1966. * Brok, F., Ramot, B., Zwang, E., and Danon, D. Enzyme activities in human red blood cells of different age groups. Isr.J.Med.Sci. 2:291-296, 1966. * Burka, E.R., Weaver III, Z., and Marks, P.A. Clinical spectrum of hemolytic anemia associated with G 6 PD deficiency. Ann.Intern.Med. 64:817-825, 1966. * Carson, P.E. and Frischer, H. Glucose-6-phosphate dehydrogenase deficiency and related disorders of the pentose phoshate pathway. Am.J.Med. 41:744-761, 1966. * Chan, T.K. G-6-PD in West Scotland. Lancet 2:752, 1966. * Charmot, G., Dodin, A., Kauffmann, J.M., Voelckel, J., Auger, C., and Mailloux, C. A report on 50 cases of glucose-6-phosphate dehydrogenase deficiency observed in hospital in Tananarive. Bull.Soc.Path.Exot. 59:400-410, 1966. * Chatterjea, J.B. Haemoglobinopathies, glucose-6-phosphate dehydrogenase deficiency and allied problems in the Indian subcontinent. Bull.WHO 35:837-856, 1966. * Cheun, L.H. Glucose-6-phosphate dehydrogenase activity in erythrocytes of experimental animals. J.Clin.Pathol. 19:614-616, 1966. * Choremis, C., Kattamis, C.H.A., Kyriazakou, M., and Gavriilidou, E. Viral hepatitis in G-6-PD deficiency. Lancet 1:269-270, 1966. * Cloutier, M.D. and Burgert, E.O. Congenital nonspherocytic hemolytic disease secondary to G-6-PD deficiency: Report of 3 cases. Mayo Clin.Proc. 41:316-325, 1966. * Crawford, M.H., Morrow, A.C., and Motulsky, A.G. Red-cell glucose-6-phosphate dehydrogenase variation in primates. Am.J.Phys.Anthropol. 24:207, 1966. * De Gowin, R.L., Eppes, R.B., Powell, R.D., and Carson, P.E. The haemolytic effects of diaphenylsulfone (DDS) in normal

subjects and in those with glucose-6-phosphate-dehydrogenase deficiency. Bull.WHO 35:165-179, 1966. * Dern, R.J. A new hereditary quantitative variant of G-6-PD characterized by a marked increase in enzyme activity. J.Lab.Clin.Med. 68:560-565, 1966. * Eppes, R., Brewer, G., De Gowin, R., McNamara, J., Flanagan, C., Schrier, S., Tarlov, A., Powell, R., and Carson, P. Oral glucose tolerance in negro men deficient in G-6-PD. N.Engl.J.Med. 275:855-861, 1966. * Fraser, G.R., Grunwald, P., and Stamatoyannopoulos, G. Glucose-6-phosphate dehydrogenase (G6PD) deficiency, abnormal haemoglobins, and thalassaemia in Yugoslavia. J.Med.Genet. 3:35-41, 1966. * Gartler, S.M., Ziprkowski, L., Krakowski, A., Ezra, R., Szeinberg, A., and Adam, A. G-6-PD mosaicism as a tracer in the study of hereditary multiple trichoepithelioma. Am.J.Hum.Genet. 18:282-287, 1966. * George, J.N., O'Brien, R.L., Pollack, S., and Crosby, W.H. Studies of in vitro primaquine hemolysis: Substrate requirement for erythrocyte membrane damage. J.Clin.Invest. 45:1280-1289, 1966. * Goswitz, F., Lee, G.R., Cartwright, G.E., and Wintrobe, M.M. Erythrocyte reduced glutathione glucose-6-phosphate dehydrogenase, and 6-phosphogluconic dehydrogenase in patients with myelofibrosis. J.Lab.Clin.Med. 67:615-623, 1966. * Grossman, A., Ramanathan, K., Justice, P., Gordon, J., Shahidi, N.T., and Hsia, D. Congenital nonspherocytic hemolytic anemia associated with erythrocyte G-6-PD deficiency in a negro family. Pediatrics 37:624-629, 1966. * Helge, H. and Borner, K. Kongenitale nichtspherozytere hemolytische Anemie, Katarakt und Glucose-6-phosphat-dehydrogenase-mangel. Dtsch.Med.Wochenschr. 91:1584-1589, 1966. * Ifekwunigwe, A.E. and Luzzatto, L. Kernicterus in G.-6-P.D.-deficiency. Lancet 1:667, 1966. * Jacob, H. and Jandl, J.H. A simple visual screening test for G-6-PD deficiency employing ascorbate and cyanide. N.Engl.J.Med. 274:1162-1167, 1966. * Justice, P., Shih, L.Y., Gordon, J., Grossman, A., and Hsia, D. Characterization of leukocyte glucose-6-phosphate dehydrogenase in normal and mutant human subjects. J.Lab.Clin.Med. 68:552-559, 1966. * Lerner, I. and Doscherholmen, A. Congenital nonspherocytic hemolytic disease. Minn.Med. 49:1387-1393, 1966. * Lisker, R., Zarate, G., and Loria, A. Studies on several genetic hematologic traits of Mexicans IX. Abnormal hemoglobins and erythrocytic glucose-6-phosphate dehydrogenase deficiency in several Indian tribes. Blood 27:2824-830, 1966. * Lu, T.C., Wei, H., and Blackwell, R.Q. Increased incidence of severe hyperbilirubinemia among newborn Chinese infants with G-6-PD deficiency. Pediatrics 37:994-999, 1966. * Mathai, C.K., Ohno, S., and Beutler, E. Sex-linkage of the glucose-6-phosphate dehydrogenase gene in Equidae. Nature 210:115-116, 1966. Notes: (B144). * McCurdy, P.R. and Donohoe, R.F. Pyridoxine-responsive anemia conditioned by isonicotinic acid hydrazide. Blood 27:352-362, 1966. * McCurdy, P.R., Kirkman, H.N., Naiman, J.L., Jim, R.T.S., and Pickard, B.M. A Chinese variant of glucose-6-phosphate

dehydrogenase. J.Lab.Clin.Med. 67:374-385, 1966. * Michot, F., Rastetter, J., and Gronauer, H. Durch Neo-salvarsan ausgelste Hemolyse bei Glukose-6-phosphat-dehydrogenase-mangel, kombiniert mit hepatischem Icterus. Schweiz.Med.Wochenschr. 96:985-987, 1966. * Motulsky, A.G., Vandepitte, J., and Fraser, G.R. Population genetic studies in the Congo. I. Glucose-6-phosphate dehydrogenase deficiency, hemoglobin S, and malaria. Am.J.Hum.Genet. 18:514-537, 1966. * Pinto, P.V.C., Newton, W.A.J., and Richardson, K.E. Evidence for four types of erythrocyte glucose-6-phosphate dehydrogenase from G-6-PD deficient human subjects. J.Clin.Invest. 45:823-831, 1966. * Powell, R., Brewer, G.J., De Gowin, R., and Carson, P. Effects of glucose-6-phosphate dehydrogenase deficiency upon the host and upon host-drug-malaria parasite interactions. Milit.Med. 131:1039-1056, 1966. * Ragab, A.H., El-Alfi, O.S., and Abboud, M.A. Incidence of glucose-6-phosphate dehydrogenase deficiency in Egypt. Am.J.Hum.Genet. 18:21-25, 1966. * Salen, G., Goldstein, F., Haurani, F., and Wirts, C.W. Acute hemolytic anemia complicating viral hepatitis in patients with glucose-6-phosphate dehydrogenase deficiency. Ann.Intern.Med. 65:1210-1220, 1966. * Sartori, E., Panizon, F., and Zacchello, F. Bimodal distribution of erythrocytes in heterozygotes for strong Mediterranean glucose-6-phosphate dehydrogenase deficiency. J.Med.Genet. 3:42-46, 1966. * Sass, M.D., Caruso, C.J., and Axelrod, D.R. Rapid screening for D-glucose-6-phosphate: NADP oxidoreductase deficiency with methylene blue. J.Lab.Clin.Med. 68:156-162, 1966. * Schmidt, P.M. Syndrome hemolytique par deficit en glucose-6-phosphate-dehydrogenase chez un Autrichien. Schweiz.Med.Wochenschr. 86:1262-1264, 1966. * Shaw, C.R. G-6-PD homologous molecules in deer mouse and man. Science 153:1013-1015, 1966. * Siniscalco, M., Filippi, G., Latte, B., Piomelli, S., Rattazzi, M., Gavin, J., Sanger, R., and Race, R.R. Failure to detect linkage between Xg and other X-borne loci in Sardinians. Ann.Hum.Genet. 29:231-252, 1966. * Siniscalco, M., Bernini, L., Filippi, G., Latte, B., Meera-Khan, P., Piomelli, S., and Rattazzi, M. Population genetics of haemoglobin variants, thalassaemia and G-6-PD deficiency, with particular reference to the malaria hypothesis. Bull.WHO 34:379-393, 1966. * Smith, J.E. and Beutler, E. Anomeric specificity of human erythrocyte glucose-6-phosphate dehydrogenase. Proc.Soc.Exp.Biol.Med. 122:671-673, 1966. Notes: (B149). * Stamatoyannopoulos, G., Panayotopoulos, A., and Motulsky, A.G. The distribution of G-6-PD deficiency in Greece. Am.J.Hum.Genet. 18:296-308, 1966. * Stuckey, W.J.J. Hemolytic anemia and erythrocyte glucose-6-phosphate dehydrogenase deficiency. Am.J.Med.Sci. 251:104-115, 1966. * Sutton, R.N.P. Viral hepatitis in G-6-PD deficiency. Lancet 1:550-551, 1966. * Waller, H.D., Lhr, G.W., and Gayer, J. Hereditere nichtspherocytere hemolytische Anemie durch Glucose-6-phosphatdehydrogenase-mangel. (Bildung eines

Enzymproteins mit verenderten Eigenschaften in den blutzellen einer Deutschen Familie). Klin.Wochenschr. 44:122-128, 1966. * Walter, H. and Caccam, J.F. Effect of oxidized glutathione on some enzymes of erythrocytes and its relation to erythrocytic enzyme activity and electrophoretic mobility. Biochem.J. 100:274-277, 1966. * Westring, D.W. and Pisciotta, A.V. Anemia, cataracts, and seizures in patient with glucose-6-phosphate dehydrogenase deficiency. Arch.Intern.Med. 118:385-390, 1966. * Yoshida, A. Glucose-6-phosphate dehydrogenase of human erythrocytes. I. Purification and characterization of normal (B+) enzyme. J.Biol.Chem. 241:4966-4976, 1966. * Bartos, H.R. and Desforges, J.F. Enzymes as erythrocyte age reference standards. Am.J.Med.Sci. 254:862-865, 1967. * Berkel, I., Say, B., Bowman, J.E., and Carson, P.E. Types of erythrocytic glucose-6-phosphate dehydrogenase in normal and in deficient Turkish subjects. Turk.J.Pediatr. 9:13-17, 1967. * Betke, K., Kleihauer, E., and Knotek, Z. Zytologische untersuchungen zur frage des zellmosaiks bei heterozygoten frauen mit glukose-6-phosphatdehydrogenase-mangel. Acta Paediatr.Scand.(Suppl) 172:30-38, 1967. * Betke, K., Beutler, E., Brewer, G.J., Kirkman, H.N., Luzzatto, L., Motulsky, A.G., Ramot, B., and Siniscalco, M. Standardization of procedures for the study of glucose-6-phosphate dehydrogenase. Report of a WHO scientific group. WHO Tech.Rep.Ser. No. 366, 1967. Notes: (B173B). * Beutler, E., Collins, Z., and Irwin, L.E. Value of genetic variants of glucose-6-phosphate dehydrogenase in tracing the origin of malignant tumors. N.Engl.J.Med. 276:389-391, 1967. Notes: (B167). * Beutler, E., Collins, Z., and Irwin, L.E. The use of electrophoretic variants of G-6-PD in determining the multicentric or unicentric origin of malignant tumors. Clin.Res. 15:110, 1967. Notes: (B161). * Beutler, E., Mathai, C., and Smith, J.E. New biochemical variants of G-6-PD giving rise to congenital nonspherocytic hemolytic disease (CNHD). Clin.Res. 15:130, 1967. Notes: (B162). * Beutler, E. Glucose-6-phosphate dehydrogenase deficiency. Diagnosis, clinical and genetic implications. Am.J.Clin.Pathol. 47:303-311, 1967. Notes: (B169). * Bowman, J.E. and Ronaghy, H. Hemoglobin, glucose-6-phosphate dehydrogenase, phosphogluconate dehydrogenase and adenylate kinase polymorphism in moslems in Iran. Am.J.Phys.Anthropol. 27:119-124, 1967. * Brewer, G.J., Gall, J.C., Honeyman, M., Gershowitz, H., Schreffler, D.C., Dern, R.J., and Hames, C. Inheritance of quantitative expression of erythrocyte glucose-6-phosphate dehydrogenase activity in the negro - a twin study. Biochem.Genet. 1:41-53, 1967. * Chernof, D. Dapsone-induced hemolysis and G 6 PD deficiency. JAMA 201:554-556, 1967. * Dausset, J. and Contu, L. Drug-induced hemolysis. In: Annu.Rev.Med. edited by De Graff, A.C. and Creger, W.P.The George Banta Co., Inc. 1967,p. 55-70. * DeGowin, R.L. A review of therapeutic and hemolytic effects of dapsone. Arch.Intern.Med. 120:242-248, 1967.

* Doyen, A., Leonard, J., Mbendi, S., and Sonnet, J. Influence des doses therapeutiques du ciba 32644-ba sur l'hematopoiese des patients atteints de bilharziose et d'amibiase. Acta Trop.(Basel) 24:59-77, 1967. * Eshaghpour, E., Oski, F.A., and Williams, M. The relationship of erythrocyte glucose-6-phosphate dehydrogenase deficiency to hyperbilirubinemia in Negro premature infants. J.Pediatr. 70:595-601, 1967. * Flatz, G. and Dueren, R. Glucose-6-phosphate dehydrogenase deficiency in Spain. Humangenetik 4:81-83, 1967. * Gelpi, A.P. Glucose-6-phosphate dehydrogenase deficiency, the sickling trait, and malaria in Saudi Arab children. Trop.Peds. 71:138-146, 1967. * George, J.N., Sears, D.A., McCurdy, P., and Conrad, M.E. Primaquine sensitivity in caucasians: Hemolytic reactions induced by primaquine in G-6-PD deficient subjects. J.Lab.Clin.Med. 70:80-93, 1967. * Gilles, H.M., Fletcher, K.A., Hendrickse, R.G., Lindner, R., Reddy, S., and Allan, N. Glucose-6-phosphate-dehydrogenase deficiency, sickling, and malaria in African children in South Western Nigeria. Lancet 1:138-140, 1967. Notes: UI - 67084885. * Haut, A. and Taylor, E.H. Catalase function in glucose-6-phosphate dehydrogenase deficiency. J.Clin.Invest. 46:1068, 1967. * Hersko, C. and Vardy, P.A. Haemolysis in typhoid fever in children with G-6-PD deficiency. BMJ 1:214-215, 1967. * Hori, S.H., Kamada, T., and Matsui, S.I. Electrophoretic separation of the magnesium-dependent glucose 6-phosphate dehydrogenases in rats. J.Histochem.Cytochem. 15:419-420, 1967. * Ideo, G., Coghe, A., and Dioguardi, N. La catalasi eritrocitaria nei soggetti normali e carenti di glucosio-6fosfato deidrogenasi: Deteminazione quantitativa dell'enzima e sua carat- terizzazione cromatografica. Haematologica (Pavia) 52:285-300, 1967. * Jim, R.T.S. Survey for erythrocyte glucose-6-phosphate dehydrogenase deficiency in Hawaii. Acta Haematol.(Basel) 37:94-99, 1967. * Kaplan, J.C., Rosa, R., Seringe, P., and Hoeffel, J.C. Le polymorphisme genetique de la glucose-6-phosphate deshydrogenase erythrocytaire chez l'homme. Enzyme 8:332-340, 1967. * Kattamis, C.A. Glucose-6-phosphate dehydrogenase deficiency in female heterozygotes and the X-inactivation hypothesis. Acta Paediatr.Scand.(Suppl) 172:103-109, 1967. * Kosower, N.S., Vanderhoff, G.A., and London, I.M. The regeneration of reduced glutathione in normal and glucose-6-phosphate dehydrogenase deficient human red blood cells. Blood 29:313-319, 1967. * Long, W.K., Wilson, S.W., and Frenkel, E.P. Associations between red cell glucose-6-phosphate dehydrogenase variants and vascular diseases. Am.J.Hum.Genet. 19:35-53, 1967. * Lothe, F. Erythrocyte glucose-6-phosphate dehydrogenase deficiency in uganda. Nature 215:299-300, 1967. * Lu, T.C. and Wei, H. Erythrocyte acid phosphomonoesterase activity in newly born Chinese deficient in glucose-6-phosphate dehydrogenase. Nature 213:707-708, 1967. * Luzzatto, L. and Okoye, V.C.N. Resolution of genetic variants of human erythrocyte glucose-6-phosphate dehydrogenase by thin layer chromatography. Biochem.Biophys.Res.Commun. 29:705-709, 1967.

* Luzzatto, L. Regulation of the activity of glucose-6-phosphate dehydrogenase by NADP+ and NADPH. Biochim.Biophys.Acta 146:18-25, 1967. * McGuinness, R. and Saunders, R.A. Erythrocyte galactose-1-phosphate uridyl transferase and glucose- 6-phosphate dehydrogenase activity in the population of the Rhondda Fach. Clin.Chim.Acta 16:221-226, 1967. * Mengel, C.E., Metz, E., and Yancey, W.S. Anemia during acute infections. Role of glucose-6-phosphate dehydrogenase deficiency in negroes. Arch.Intern.Med. 119:287-290, 1967. * Messerschmitt, J., Suaudeau, C., Benallegue, V.R., Fabre, S., Bon, J., Andre, L., Khati, B., Dubois, M., Benabdallah, S., and Kotchoyan, P. Defaut en G-6-PD et anemies hemolytiques en Algerie. Nouv.Rev.Fr.Hematol. 7:827-840, 1967. * Omar, M.E.S. and Wahab, M.F.A. Treatment of typhoid and paratyphoid fever with furazolidone. J.Trop.Med.Hyg. 70:43-45, 1967. * Pryor, D.S. and Pitney, W.R. Hereditary elliptocytosis: A report of two families from New Guinea. Br.J.Haematol. 13:126-134, 1967. * Rattazzi, M.C., Bernini, L.F., Fiorelli, G., and Mannucci, P.M. Electrophoresis of glucose-6-phosphate dehydrogenase: A new technique. Nature 213:79-80, 1967. * Rosta, J., Makoi, Z., and Reif, M. Investigations regarding glucose-6-phosphate dehydrogenase deficiency in Hungary. Acta Paediatr.Acad.Sci.Hung. 8:41-51, 1967. * Salvidio, E., Pannacciulli, I., Tizianello, A., and Ajmar, F. Nature of hemolytic crises and the fate of G-6-PD deficient, drug-damaged erythrocytes in Sardinians. N.Engl.J.Med. 276:1339-1344, 1967. * Salvidio, E., Pannacciulli, I., and Tizianello, A. La capacita erritropoietica dei soggetti con deficienza di G 6 PD eritrocitaria. Atti.Accad.Med.Lomb. 22:16-18, 1967. * Sass, M.D., Caruso, C.J., and Axelrod, D.R. Accumulation of methylene blue by metabolizing erythrocytes. J.Lab.Clin.Med. 69:447-455, 1967. * Schettini, F. and Meloni, T. Characterization of glucose-6-phosphate dehydrogenase in Sardinian children with congenital nonspherocytic haemolytic anaemia. Acta Haematol.(Basel) 37:198-205, 1967. * Schrter, W., Drescher, J., and Fischer, K. ber eine seltene Form des Glucose-6-phosphatdehydrogenase-mangels mit kongenitaler nichtspherocyterer hemolytische Anemie. Klin.Wochenschr. 45:355-362, 1967. * Srivastava, S.K. and Beutler, E. Permeability of normal and glucose-6-phosphate dehydrogenase deficient erythrocytes to glutathione. Biochem.Biophys.Res.Commun. 28:659-664, 1967. Notes: (B174). * Stamatoyannopoulos, G., Papayannopoulou, T.H., Bakopoulos, C.H.R., and Motulsky, A.G. Detection of glucose-6-phosphate dehydrogenase deficient heterozygotes. Blood 29:87-101, 1967. * Stamatoyannopoulos, G., Yoshida, A., Bacopoulos, C., and Motulsky, A. Athens variant of glucose-6-phosphate dehydrogenase. Science 157:831-833, 1967. * Sulyok, E. and Cholnoky, P. The role of erythrocyte glucose-6-phosphate dehydrogenase deficiency in icterus gravis neonatorum. Acta Paediatr.Acad.Sci.Hung. 8:323-326, 1967. * Vargas, L.P. and Gonzales, C.S. Haemolytic anaemia after nalidixic acid. Lancet 2:97-98, 1967. * Vergnes, H. and Larrouy, G. Les deficits en G6PD dans les

populations des Andes boliviennes. Soc.Franc.D'hemat. 7:124-128, 1967. * Wasi, P., Na-Nakorn, S., and Suingdumrong, A. Studies of the distribution of haemoglobin E, thalassaemias and glucose-6-phosphate dehydrogenase deficiency in North-Eastern Thailand. Nature 214:501-502, 1967. * Werth, G. and Mueller, G. Vererbbarer Glucose-6-phosphatdehydrogenasemangel in den Erythrocyten von Ratten. Klin.Wochenschr. 45:265-269, 1967. * Yoshida, A. Human glucose-6-phosphate dehydrogenase: Purification and characterization Hematology. Biochem.Genet. 1:81-99, 1967. * Yoshida, A., Stamatoyannopoulos, G., and Motulsky, A. Negro variant of glucose-6-phosphate dehydrogenase deficiency (A-) in man. Science 155:97-99, 1967. * Yoshida, A. A single amino acid substitution (asparagine to aspartic acid) between normal (B+) and the common negro variant (A+) of human glucose-6-phosphate dehydrogenase. Proc.Natl.Acad.Sci.USA 57:835-840, 1967. * Yoshida, A., Steinmann, L., and Harbert, P. In vitro hybridization of normal and variant human glucose-6-phosphate dehydrogenase. Nature 216:275-276, 1967. * Ziai, M., Amirhakimi, G.H., Reinhold, J.G., Tabatabee, M., Gettner, M.E., Bowman, J.E., and Kamal, D. Malaria prophylaxis and treatment in G-6-PD deficiency. Clin.Pediatr. 6:242-243, 1967. * Abe, T., Takafuji, H., Yamamoto, M., Daimon, S., Nakajima, K., Agasawara, K., Takino, T., Fujiki, N., Nishina, T., and Miwa, S. Kongenitale nichtspherozytare hemolytische Anemien durch Mangel an Glucose-6-phosphat-dehydrogenase der Erythrozyten in einer Japanischen. Blut 17:143-151, 1968. * Arcuri, F. and Robert, L. Anemia emolitica acuta in corso di sepsi da proteus morganii in soggetto carente di glucoso - 6 - fosfato deidrogenasi eritrocitaria. Arch.E.Maragliano Patol.Clin. 24:347-358, 1968. * Azevedo, E., Kirkman, H.N., Morrow, A.C., and Motulsky, A.G. Variants of red cell glucose-6-phosphate dehydrogenase among Asiatic Indians. Ann.Hum.Genet. 31:373-379, 1968. * Beutler, E. Test for glucose-6-phosphate dehydrogenase deficiency. Pediatrics 73:297, 1968. Notes: (B238). * Beutler, E., Mathai, C.K., and Smith, J.E. Biochemical variants of glucose-6-phosphate dehydrogenase giving rise to congenital nonspherocytic hemolytic disease. Blood 31:131-150, 1968. Notes: (B188). * Beutler, E. and Mitchell, M. Special modifications of the fluorescent screening method for glucose-6-phosphate dehydrogenase deficiency. Blood 32:816-818, 1968. Notes: (B203). * Beutler, E. Abnormalities of glycolysis (HMP shunt). Bibl.Haematol. 29:146-157, 1968. Notes: (B155). * Beutler, E. The genetics of glucose-6-phosphate dehydrogenase deficiency. In: Hereditary Disorders of Erythrocyte Metabolism, edited by Beutler, E.New York:Grune & Stratton, Inc. 1968,p. 114-125. Notes: (B185). * Blackwell, R.Q., Ro, I.H., and Yen, L. Low incidence of erythrocyte G-6-PD deficiency in Koreans. Vox Sang. 14:299-303,

1968. * Brown, W.R. and Boon, W.H. Hyperbilirubinemia and kernicterus in glucose-6-phosphate dehydrogenase-deficient infants in Singapore. Pediatrics 41:1055-1062, 1968. * Chat, L.X., Quang, L.S., Humbert, C., and Giao, C.Q. Le deficit en glucose-6-phosphate dehydrogenase au Viet-nam. Nouv.Rev.Fr.Hematol. 8:878-884, 1968. * Criss, W.E. and McKerns, K.W. Purification and partial characterization of glucose 6-phosphate dehydrogenase from cow adrenal cortex. Biochemistry 7:125-134, 1968. * De Mars, R. A temperature-sensitive glucose-6-phosphate dehydrogenase in mutant cultured human cells. Proc.Natl.Acad.Sci.USA 61:562-569, 1968. * Deshmukh, V.V. and Sharma, K.D. Deficiency of erythrocyte glucose-6-phosphate dehydrogenase and sickle cell. Indian J.Med.Res. 56:821-825, 1968. * Doeblin, T.D., Ingall, G.B., Pinkerton, P.H., Dronamraju, K.R., and Bannerman, R.M. Genetic studies of the Seneca indians: Haptoglobins, transferrins, G-6-PD deficiency, hemoglobinopathy, color blindness, morphological traits and dermatoglyphics. Acta Genet. 18:251-260, 1968. * Fairbanks, V.F. and Lampe, L.T. A tetrazolium-linked cytochemical method for estimation of glucose-6-phosphate dehydrogenase activity in individual erythrocytes: Applications in the study of heterozygotes for glucose-6-phosphate dehydrogenase deficiency. Blood 31:589-603, 1968. * Fernandez, M. and Fairbanks, V.F. Glucose-6-phosphate dehydrogenase deficiency in the Philippines: Report of a new variant-- G 6 PD Panay. Mayo Clin.Proc. 43:645-660, 1968. * Gandini, E., Gartler, S.M., Angione, G., Argiolas, N., and Dell Acqua, G. Developmental implications of multiple tissue studies in glucose- 6-phosphate dehydrogenase-deficient heterozygotes. Proc.Natl.Acad.Sci.USA 61:945-948, 1968. * Haywood, B., Starkweather, W., Spencer, H., and Zarafonetis, C. Electrophoretic separation of glucose-6-phosphate dehydrogenase from human erythrocytes with agar gels. J.Lab.Clin.Med. 71:324-327, 1968. * Hook, E.B., Stamatoyannopoulos, G., Yoshida, A., and Motulsky, A.G. Glucose-6-phosphate dehydrogenase Madrona: A slow electrophoretic glucose-6-phosphate dehydrogenase variant with kinetic characteristics similar to those of normal type. J.Lab.Clin.Med. 72:404-409, 1968. * Kirkman, H.N., Kidson, C., and Kennedy, M. Variants of human glucose-6-phosphate dehydrogenase. Studies of samples from New Guinea. In: Hereditary Disorders of Erythrocyte Metabolism, edited by Beutler, E.New York:Grune & Stratton, Inc. 1968,p. 126-145. * Kissin, C. and Beutler, E. The utilization of glucose by normal glucose-6-phosphate dehydrogenase and by glucose-6-phosphate dehydrogenase Mediterranean. Proc.Soc.Exp.Biol.Med. 128:595-601, 1968. Notes: (B196). * Komma, D.J. Glucose-6-phosphate dehydrogenase in drosophila: A sex-influenced electrophoretic variant. Biochem.Genet. 1:229-237, 1968. * Lai, H.C., Lai, M.P.Y., and Leung, K.S.N. Glucose-6-phosphate dehydrogenase deficiency in Chinese. J.Clin.Pathol. 21:44-47, 1968. * Liebowitz, J. and Cohen, G. Increased hydrogen peroxide levels in glucose-6-phosphate dehydrogenase deficient

erythrocytes exposed to acetylphenylhydrazine. Biochem.Pharmacol. 17:983-988, 1968. * Luzzatto, L. and Afolayan, A. Different types of human erythrocyte glucose-6-phosphate dehydrogenase, with characterization of two new genetic variants. J.Clin.Invest. 47:1833-1842, 1968. * Luzzatto, L. and Allan, N.C. Relationship between the genes for glucose-6-phosphate dehydrogenase and for hemoglobin in a Nigerian population. Nature 219:1041-1042, 1968. * Marti, H.R. Semiquantitative assay of erythrocyte glucose-6-phosphate dehydrogenase activity by a new modification of the Motulsky test. Experientia 24:416, 1968. * Necheles, T.F. and Gorshein, D. Virus-induced hemolysis in erythrocytes deficient in glucose-6-phosphate dehydrogenase. Science 160:535-537, 1968. * Norden, C.W., Desforges, J.F., and Kass, E.H. Hemolytic effect of sulfonamides in patients with erythrocytes deficient in glucose-6-phosphate dehydrogenase. N.Engl.J.Med. 279:30-31, 1968. * Park, I. and Jones, H.W.J. Glucose-6-phosphat dehydrogenase and the histogenesis of epidermoid carcinoma of the cervix. Am.J.Obstet.Gynecol. 102:106-109, 1968. * Pelz, L. and Wutschke, H. SeX-chromatin und glucose-6-phosphatdehydrogenase-aktivitat bei neugeborenen. Humangenetik 6:259-260, 1968. * Peterson, W.D.J., Stulberg, C.S., Swanborg, N.K., and Robinson, A.R. Glucose-6-phosphate dehydrogenase isoenzymes in human cell cultures determined by sucrose-agar gel and cellulose acetate zymograms. Proc.Soc.Exp.Biol.Med. 128:772-776, 1968. * Piomelli, S., Corash, L.M., Davenport, D.D., Miraglia, J., and Amorosi, E.L. In vivo lability of glucose-6-phosphate dehydrogenase in GdA-and Gd Mediterranean deficiency. J.Clin.Invest. 47:940-948, 1968. * Prasad, A.S., Tranchida, L., Konno, E.T., Berman, L., Albert, S., Sing, C., and Brewer, G.J. Hereditary sideroblastic anemia and glucose-6-phosphate dehydrogenase deficiency in a negro family. J.Clin.Invest. 47:1415-1424, 1968. * Puxeddu, A., Santeusanio, F., Migliorini, E., Siracusa, A., and Merlitti, A. Studio di un gruppo familiare umbro-marchigiano con anemia emolitica congenita non sferocitica da carenza di glucosio-6-fosfato-deidrogenasi (G6-PD). Haematol.Arch. 53:30-52, 1968. * Rajkondawar, V.L., Modi, T.H., and Mishra, S.N. Drug induced acute haemolytic anaemia in glucose-6-phosphate dehydrogenase deficiency subjects. J.Assoc.Physicians (India) 16:589-593, 1968. * Rattazzi, M.C. Glucose-6-phosphate dehydrogenase from human erythrocytes: Molecular weight determination by gel filtration. Biochem.Biophys.Res.Commun. 31:16-24, 1968. * Restrepo, M.A. and Gutierrez, E. The frequency of glucose-6-phosphate dehydrogenase deficiency in Colombia. Am.J.Hum.Genet. 20:82-85, 1968. * Russo, G., Schiliro, G., and Gallone, G. L'attivita catalasica di globuli rossi carenti in glucosio-6-fosfato deidrogenasi. Pediatria (Napoli) 76:169-177, 1968. * Schneer, J.H. A survey for erythrocyte glucose-6-phosphate dehydrogenase deficiency in Rumania. Acta Haematol.(Basel) 40:44-47, 1968. * Smith, J.E. Low erythrocyte glucose-6-phosphate dehydrogenase activity and primaquine insensitivity in sheep. J.Lab.Clin.Med. 71:826-833, 1968.

* Soldin, S.J. and Balinsky, D. The kinetic properties of human erythrocyte glucose-6-phosphate dehydrogenase. Biochemistry 7:1077-1082, 1968. * Srivastava, S.K. and Beutler, E. Elevated levels of oxidized glutathione (GSSG) in G-6-PD deficient red cells. Clin.Res. 16:125, 1968. Notes: (B186). * Srivastava, S.K. and Beutler, E. Oxidized glutathione levels in erythrocytes of glucose-6-phosphate dehydrogenase-deficient subjects. Lancet 2:23-24, 1968. Notes: (B197). * Stern, L., Cameron, D., and Dallaire, L. Neonatal jaundice associated with erythrocyte glucose-6-phosphate dehydrogenase deficiency in a non-Mediterranean caucasian infant with trisomic Down's syndrome. Can.Med.Assoc.J. 98:1196-1197, 1968. * Sulis, E. and Spano, G. Osservazioni preliminari sull'incidenza neoplastica e sul comportamento enzimatico e proliferativo del tessuto tumorale negli individui carenti di glucosio-6-fosfato deidrogenasi (G-6-PD). Boll.Soc.Ital.Biol.Sper. 44:1246-1249, 1968. * Tchernia, G., Najean, Y., Schaison, G., Boivin, P., Scialom, C., Rullier, J., and Bernard, J. Deficit complet en glucose-6-phosphate-deshydrogenase associe a une cholemie familiale de gilbert. Arch.Fr.Pediatr. 25:621-637, 1968. * Tizianello, A., Pannacciulli, I., Ajmar, F., and Salvidio, E. Sites of destruction of red cells in G-6-PD deficient caucasians and in phenylhydrazine treated patients. Scand.J.Haematol. 5:116-128, 1968. * Tuchinda, S., Rucknagel, D.L., Na-Nakorn, S., and Wasi, P. The Thai variant and the distribution of alleles of 6-phosphogluconate dehydrogenase and the distribution of glucose-6-phosphate dehydrogenase deficiency in Thailand. Biochem.Genet. 2:253-264, 1968. * Weinreich, J., Busch, D., Gottstein, U., Schaefer, J., and Rohr, J. ber zwei neue Felle von herediterer nichtspherocyterer hemolytischer Anemie bei Glucose-6-phosphat-dehydrogenase-defekt in einer Nord Deutschen Familie. Klin.Wochenschr. 46:146-149, 1968. * Westring, D.W. and Calas, C. Hemolytic effect of estrogen on G-6-PD deficient erythrocytes. Clin.Res. 16:544, 1968. * Whelton, A., Donadio, J.V.J., and Elisberg, B.L. Acute renal failure complicating rickettsial infections in glucose-6-phosphate dehydrogenase-deficient individuals. Ann.Intern.Med. 69:323-328, 1968. * Yoshida, A. Subunit structure of human glucose-6-phosphate dehydrogenase and its genetic implication. Biochem.Genet. 2:237-243, 1968. * Yoshida, A. The structure of normal and variant human glucose-6-phosphate dehydrogenase. In: Hereditary Disorders of Erythrocyte Metabolism, edited by Beutler, E.New York:Grune & Stratton, Inc. 1968,p. 146-164. * Yoshida, A., Stamatoyannopoulos, G., and Motulsky, A.G. Biochemical genetics of glucose-6-phosphate dehydrogenase variation. Ann.NY Acad.Sci. 155:868-879, 1968. * Abrahamov, A., Freier, S., and Goldstein, R. Incidence of hemolysis in acute infections among G-6-PD deficient children. Harefuah 77:180-181, 1969. * Arcuri, F. and Robert, L. Anemia emolitica acuta in corso di sepsi da proteus morganii in soggetto carente di glucosio-6-fosfato deidrogenasi eritocitaria. Giornale de

Malattie Infettive 21:257, 1969. * Azevedo, E.S. and Yoshida, A. Brazilian variant of glucose-6-phosphate dehydrogenase (Gd Minas Gerais). Nature 222:380-382, 1969. * Bannert, N., Thal, W., and Lubas, E. Glucose-6-phosphatdehydrogenase-mangel als ursache des hemolytischen ikterus bei einer deutschen familie. Monatsschr.Kinderheilkd. 117:675-679, 1969. * Ben-Bassat, J. and Ben-Ishay, D. Hereditary hemolytic anemia associated with glucose-6-phosphate dehydrogenase deficiency (Mediterranean type). Isr.J.Med.Sci. 5:1053-1059, 1969. * Beutler, E. Drug-induced hemolytic anemia. Pharmacol.Rev. 21:73-103, 1969. Notes: (B208). * Beutler, E. G-6-PD activity of individual erythrocytes and X-chromosomal inactivation. In: Biochemical Methods in Red Cell Genetics, edited by Yunis, J.J.New York:Academic Press, Inc. 1969,p. 95-113. Notes: (B206). * Botha, M.C., Dern, R.J., Mitchell, M., West, C., and Beutler, E. G6PD Capetown, a variant of glucose-6-phosphate dehydrogenase. Am.J.Hum.Genet. 21:547-551, 1969. Notes: (B236). * Clearfield, H.R., Brody, J.I., and Tumen, H.J. Acute viral hepatitis, glucose-6-phosphate dehydrogenase deficiency, and hemolytic anemia. Arch.Intern.Med. 123:689-691, 1969. * Cohen, P. and Rosemeyer, M.A. Subunit interactions of glucose-6-phosphate dehydrogenase from human erythrocytes. Eur.J.Biochem. 8:8-15, 1969. * Dern, R.J., McCurdy, P.R., and Yoshida, A. A new structural variant of glucose-6-phosphate dehydrogenase with a high production rate (G6PD). J.Lab.Clin.Med. 73:283-290, 1969. * Doery, J.C.G., Hirsh, J., and DeGruchy, G.C. Erythrocyte and platelet glucose 6-phosphate dehydrogenase in normal and mutant caucasians. Scand.J.Haematol. 6:5-9, 1969. * Fairbanks, V.F. and Fernandez, M.N. The identification of metabolic errors associated with hemolytic anemia. JAMA 208:316-320, 1969. * Fung, R.H.P., Keung, Y.K., and Chung, G.S.H. Screening of pyruvate kinase deficiency and G6PD deficiency in Chinese newborn in Hong Kong. Arch.Dis.Child. 44:373-376, 1969. * Gabbas, F., Contu, L., and Mosca, A. Su un caso di epatite virale complicata da grave anemia emolitica emoglobinurica e blocco renale in un bambino con difetto di g.6.P.D. Ann.Ital.Pediatr. 22:125-132, 1969. * Gandini, E. and Gartler, S.M. Glucose-6-phosphate dehydrogenase mosaicism for studying the development of blood cell precursors. Nature 224:599-600, 1969. * Kirkman, H.N. and Luan-Eng, L.-I. Variants of glucose 6 phosphate dehydrogenase in Indonesia. Nature 221:959-960, 1969. * Kirkman, H.N., Ramot, B., and Lee, J.T. Altered aggregational properties in a genetic variant of human glucose-6-phosphate dehydrogenase. Biochem.Genet. 3:137-150, 1969. * Kuehboeck, V.J., Pietschmann, H., and Rothenbuchner, G. Enzymopenische hemolytische anemie bei einer sterreichischen familie. Wien.Klin.Wochenschr. 81:135-137, 1969. * Lenzerini, L., Meera Khan, P., Filippi, G., Rattazzi, M.C., Ray, A.K., and Siniscalco, M. Characterization of glucose-6-phosphate dehydrogenase variants. I. Occurrence of a

G6PD Seattle-like variant in Sardinia and its interaction with the G6PD Mediterranean variant. Am.J.Hum.Genet. 21:142-153, 1969. * Linder, D. Gene loss in human teratomas. Proc.Natl.Acad.Sci.USA 63:699-704, 1969. * Louderback, A., Beutler, E., Natland, M., and Temianka, D. Agar gel electrophoresis of G-6-PD isoenzymes. Clin.Res. 17:149, 1969. Notes: (B224). * Luzzatto, L., Usanga, E.A., and Reddy, S. Glucose 6-phosphate dehydrogenase deficient red cells: Resistance to infection by malarial parasites. Science 164:839-842, 1969. * Nabholz, M., Miggiano, V., and Bodmer, W. Genetic analysis with human-mouse somatic cell hybrids. Nature 223:358-363, 1969. * Nixon, A.D. and Buchanan, J.G. Survey for erythrocyte glucose-6-phosphate dehydrogenase deficiency in Polynesians. Am.J.Hum.Genet. 21:305-309, 1969. * Oertel, G.W. and Rubelein, I. Effects of dehydroepiandrosterone and its conjugates upon the activity of glucose-6-phosphate dehydrogenase in human erythrocytes. Biochim.Biophys.Acta 184:459-460, 1969. * Pannacciulli, I., Salvidio, E., Tizianello, A., and Parravidino, G. Hemolytic effects of standard single dosages of primaquine and chloroquine on G-6-PD-deficient Caucasians. J.Lab.Clin.Med. 74:653-661, 1969. * Phillips, S.M. and Silvers, N.P. Glucose-6-phosphate dehydrogenase deficiency, infectious hepatitis, acute hemolysis, and renal failure. Ann.Intern.Med. 70:99-104, 1969. * Piomelli, S. and Siniscalco, M. The haematological effects of glucose-6-phosphate dehydrogenase deficiency and thalassaemia trait: Interaction between the two genes at the phenotype level. Br.J.Haematol. 16:537-549, 1969. Notes: Anemia documented in G6PD deficiency. * Ramot, B., Brok-Simoni, F., and Ben-Bassat, I. Glucose-6-phosphate dehydrogenase, hexokinase activities and ATP levels as a function of cell density in thalassemia and iron deficiency anemia. Ann.NY Acad.Sci. 165:400-406, 1969. * Ramot, B., Ben-Bassat, I., and Shchory, M. New glucose-6-phosphate dehydrogenase variants observed in Israel and their association with congenital nonspherocytic hemolytic disease. J.Lab.Clin.Med. 74:895-901, 1969. * Rattazzi, M.C. Isolation and purification of human erythrocyte glucose-6-phosphate dehydrogenase from small amounts of blood. Biochim.Biophys.Acta 181:1-11, 1969. * Rattazzi, M.C., Lenzerini, L., Khan, P.M., and Luzzatto, L. Characterization of glucose-6-phosphate dehydrogenase variants. II. G6PD Kephalonia, G6PD Attica, and G6PD "Seattle-like" found in Greece. Am.J.Hum.Genet. 21:154-167, 1969. * Rosa, R. and Dreyfus, J.C. Hybridation de la glucose-6-phosphate deshydrogenase des globules rouges et des globules blancs humains avec l'enzyme de differents tissus de rat. Clin.Chim.Acta 24:199-202, 1969. * Saldanha, P.H., Nobrega, F.G., and Maia, J.C.C. Distribution and hereditary of erythrocyte G6PD activity and electrophoretic variants among different racial groups at Sao Paulo,Brazil. J.Med.Genet. 6:48-54, 1969. Notes: 60/60 "white" males and 25/27 females were G6PD B. 2/27 females were AB. * Salvidio, E., Pannacciulli, I., Stangoni, A., Ajmar, F., Paravidino, G., Gaetani, G., and Marogna, G. I difetti enzymatici eritrocitari nella pratica trasfusionale. Trasfusione Sangue

14:175-199, 1969. * Siniscalco, M., Klinger, H.P., Eagle, H., Koprowski, H., Fujimoto, W.Y., and Seegmiller, J.E. Evidence for intergenic complementation in hybrid cells derived from two human diploid strains each carrying an X-linked mutation. Proc.Natl.Acad.Sci.USA 62:793-799, 1969. * Smits, H.L., Oski, F.A., and Brody, J.I. The hemolytic crisis of sickle cell disease: The role of glucose-6-phosphate dehydrogenase deficiency. J.Pediatr. 74:544-551, 1969. * Sparkes, R.S., Baluda, M.C., and Townsend, D.E. Detection of glucose-6-phosphate dehydrogenase by fluorescence after cellulose acetate electrophoresis. Anal.Biochem. 30:289-292, 1969. * Sparkes, R.S., Baluda, M.C., and Townsend, D.E. Cellulose acetate electrophoresis of human glucose-6-phosphate dehydrogenase. J.Lab.Clin.Med. 73:531-534, 1969. * Talalak, P. and Beutler, E. G-6-PD Bangkok: A new variant found in congenital nonspherocytic hemolytic disease (CNHD). Blood 33:772-776, 1969. Notes: (B212). * Tan, I.K. and Whitehead, T.P. Automated fluorometric determination of glucose-6-phosphate dehydrogenase (G 6 PD) and 6-phosphogluconate dehydrogenase (6PGD) activities in red blood cells. Clin.Chem. 15:467-478, 1969. * Tanaka, K.R. and Beutler, E. Hereditary hemolytic anemia due to glucose-6-phosphate dehydrogenase Torrance: A new variant. J.Lab.Clin.Med. 73:657-667, 1969. Notes: (B215). * Valaes, T., Karaklis, A., Stravrakakis, D., Bavela-Stravrakakis, K., Perakis, A., and Doxiadis, S.A. Incidence and mechanism of neonatal jaundice related to glucose-6-phosphate dehydrogenase deficiency. Pediatr.Res. 3:448-458, 1969. * Yoshida, A. Genetic variants of human glucose 6-phosphate dehydrogenase. Jpn.J.Human Genet. 1:258-265, 1969. * Zaidman, J. On the heterogeneity of hemoglobin from normal and glucose-6-phosphate dehydrogenase-deficient individuals. Clin.Chim.Acta 23:67-73, 1969. * Zurcher, C., Kuijlman, F.F., Sass, F., Zurcher, T., Loos, J.A., and Prins, H.K. Glucose-6-phosphate dehydrogenase deficiency in females, diagnosed by partial inhibition of glutathione reductase activity in the erythrocytes after incubation with chromate. Clin.Chim.Acta 25:139-146, 1969. * Adamson, J.E., Taddeo, R.J., and Gwyn, P.P. Loss of flaps due to glucose-6-phosphate dehydrogenase deficiency. Plast.Reconstr.Surg. 46:301-304, 1970. * Barretto, O.C.O. Erythrocyte glucose-6-phosphate dehydrogenase deficiency in Sao Paulo, Brazil. Rev.Bras.Pesqui.Med.Biol. 3:61-65, 1970. * Beiguelman, B., Colli-Inglez, G., Bonder-Itskan, S., and Saldanha, P.H. Glucose-6-phosphate dehydrogenase activity among caucasoid twins. Hum.Hered. 20:535-539, 1970. * Bellanti, J.A., Cantz, B.E., and Schlegel, R.J. Accelerated decay of glucose-6-phosphate dehydrogenase activity in chronic granulomatous disease. Pediatr.Res. 4:405-411, 1970. * Benhr, H.C., Usener, H., and Wagner, H. Spontaneous haemolysis in a patient with glucose-6-phosphate dehydrogenase deficiency (mediterranean type) and heterozygote beta thalassemia. Med.Welt. 24:1091-1095, 1970. * Benhr, H.C. and Waller, H.D. Eigenschaften der

Glucose-6-P-dehydrogenase Typ "Tubingen". Klin.Wochenschr. 48:71-74, 1970. * Beutler, E. Genetic variability of G-6-PD. Humangenetik 9:250-253, 1970. Notes: (B254). * Beutler, E. and Rosen, R. Nonspherocytic congenital hemolytic anemia due to a new G-6-PD variant: G-6-PD Alhambra. Pediatrics 45:230-235, 1970. Notes: (B244). * Beutler, E. Glucose-6-phosphate dehydrogenase deficiency. Br.J.Haematol. 18:117-121, 1970. Notes: (B248). * Brinster, R.L. Glucose 6-phosphate dehydrogenase activity in the early rabbit and mouse embryo. Biochem.Genet. 4:669-676, 1970. * Busch, D. and Boie, K. Glucose-6-phosphate-dehydrogenase-defect in Deutschland. II. Eigenschaften des Enzyms (Typ Freiburg). Klin.Wochenschr. 48:74-78, 1970. * Cauchi, M.N. The incidence of glucose-6-phosphate dehydrogenase deficiency and thallassemia in Malta. Br.J.Haematol. 18:101-106, 1970. * Deiss, A., Lee, G.R., and Cartwright, G.E. Hemolytic anemia in Wilson's disease. Ann.Intern.Med. 73:413-418, 1970. * Elian, M. Epilepsy and G-6-PD deficiency. Lancet 1:364, 1970. * Engstrom, P.F. and Beutler, E. G-6-PD Tripler: A unique variant associated with chronic hemolytic disease. Blood 36:10-13, 1970. Notes: (B253). * Fialkow, P.J., Klein, G., Gartler, S.M., and Clifford, P. Clonal origin for individual Burkitt tumours. Lancet 1:384-386, 1970. * Flatz, G. Enhanced binding of FAD to glutathione reductase in G-6-PD deficiency. Nature 226:755, 1970. * Flatz, G. and Simmersbach, F. Flavin adenine dinucleotide concentration in erythrocytes with normal and deficient glucose-6-phosphate dehydrogenase. Klin.Wochenschr. 48:1071-1072, 1970. * Flatz, G. and Tantachamboon, T. Glucose-6-phosphate dehydrogenase in the population of Northern Thailand: Evidence for two common electrophoretic variants with deficient enzyme activity. Humangenetik 10:335-339, 1970. * Flatz, G., Voss, B., and Voss, S. Zur Anwendung von Sulfamethoxypyrazin bei Personen mit Mangel der Glucose-6-phosphat-dehydrogenase der Erythrocyten. Klin.Wochenschr. 48:88-91, 1970. * Hasan, N.W., Burney, A., and Mrza, A. Furazolidone therapy in typhoid fever. J.Pakistan Med.Assoc. 20:347-351, 1970. * Herz, F., Kaplan, E., and Scheye, E.S. Diagnosis of erythrocyte glucose-6-phosphate dehydrogenase deficiency in the negro male despite hemolytic crisis. Blood 35:90-93, 1970. * Holzmann, H., Morsches, B., Menzel, P., and Oertel, G.W. Sex dependence of G-6-PDH activity in human erythrocytes. Klin.Wochenschr. 48:953-954, 1970. * Huskisson, E.C., Murphy, B., and West, C. Glucose-6-phosphate dehydrogenase deficiency and chronic haemolysis in an English family. J.Clin.Pathol. 23:135-139, 1970. * Kaplan, J.C., Hanlickova-Leroux, A., Nicholas, A.M., Rosa, R., Weiler, C., and Lepercq, G. A new glucose-6-phosphate

dehydrogenase variant (G6PD Port-Royal). Enzyme 12:25-32, 1970. * Kattamis, C.A. and Tjortjatou, F. The hemolytic process of viral hepatitis in children with normal or deficient glucose-6-phosphate dehydrogenase activity. J.Pediatr. 77:422-430, 1970. * Kessler, I.I. A genetic relationship between diabetes and cancer. Lancet 1:218-220, 1970. * Kissin, C. and Cotte, J. Etude d'un variant de glucose-6-phosphate deshydrogenase: Le type Constantine. Enzyme 11:277-284, 1970. * Kosower, N.S. and Kosower, E.M. Molecular basis for selective advantage of glucose-6-phosphate-dehydrogenase-deficient individuals exposed to malaria. Lancet 2:1343-1344, 1970. * Kruatrachue, M., Sadudee, N., and Sriripanich, B. Glucose-6-phosphate-dehydrogenase-deficiency and malaria in Thailand: The comparison of parasite densities and mortality rates. Ann.Trop.Med.Parasitol. 64:11-14, 1970. * Lesobre, B., Homberg, J.C., Macon, W.R., Kourilsky, R., and Pieron, R. G-6-PD deficiency revealed during PAS therapy. Sem.Hop.Paris 46:1361-1368, 1970. * Linder, D. and Power, J. Further evidence for post-meiotic origin of teratomas in the human female. Ann.Hum.Genet. 34:21-30, 1970. * Lwanga, D. and Wing, A.J. Renal complications associated with typhoid fever. East Afr.Med.J. 47:146-152, 1970. * Mandal, B.K. and Stevenson, J. Haemolytic crisis produced by nalidixic acid. Lancet 1:614-Letter, 1970. * Manzler, A.D. and Schreiner, A.W. Copper-induced acute hemolytic anemia. A new complication of hemodialysis. Ann.Intern.Med. 73:409-412, 1970. * Mayer, K. and Ley, A.B. Hemolysis of red cells due to sulfone. Ann.Intern.Med. 72:711-714, 1970. * McCurdy, P.R. and Mahmood, L. Red cell glucose-6-phosphate dehydrogenase deficiency in Pakistan. J.Lab.Clin.Med. 76:943-948, 1970. * McCurdy, P.R., Blackwell, R.Q., Todd, D., Tso, S.C., and Tuchinda, S. Further studies on glucose-6-phosphate dehydrogenase deficiency in Chinese subjects. J.Lab.Clin.Med. 75:788-797, 1970. * Meyer, H.A. Therapeutic results with Bactrim in typhoid fever, paratyphoid fever, and other salmonelloses. Schweiz.Med.Wochenschr. 100:1493-1497, 1970. * Moskowitz, R.M. Autoimmune hemolytic anemia in a patient with a deficiency of red cell glucose-6-phosphate dehydrogenase activity. Johns Hopkins Med.J. 126:139-145, 1970. * Musumeci, S. and Mazzone, D. Studio della sopravvivenza eritrocitaria in bambini siciliani portatori di carenza di g6fd. Pediatria (Napoli) 78:868-878, 1970. * Naik, S.N. and Anderson, D.E. G-6-PD deficiency and cancer. Lancet 1:1060-1061, 1970. * Nobrega, F.G., Maia, J.C.C., Colli, W., and Saldanha, P.H. Heterogeneity of erythrocyte glucose-6-phosphate dehydrogenase (G6PD, E.C. 1.1.1.49) Activity and electrophoretic patterns among representatives of different classes of vertebrates. Comp.Biochem.Physiol. 33:191-199, 1970. * Nyhan, W.L., Bakay, B., Connor, J.D., Marks, J.F., and Keele, D.K. Hemizygous expression of glucose-6-phosphate dehydrogenase in erythrocytes of heterozygotes for the Lesch-Nyhan syndrome. Proc.Natl.Acad.Sci.USA 65:214-218, 1970. * Oni, S.B., Osunkoya, B.O., and Luzzatto, L. Paroxysmal

nocturnal hemoglobinuria: Evidence for monoclonal origin of abnormal red cells. Blood 36:145-152, 1970. * Orlina, A.R., Josephson, A.M., and McDonald, B.J. The poststorage viability of glucose-6-phosphate dehydrogenase-deficient erythrocytes. J.Lab.Clin.Med. 75:930-936, 1970. * Pawlak, A.L., Zagorski, Z., Rozynkowa, D., and Horst, A. Polish variant of glucose-6-phosphate dehydrogenase (G-6-PD Lublin). Humangenetik 10:340-343, 1970. * Pellicer, A. and Casado, A. Frequency of thalassemia and G-6-PD deficiency in five provinces of Spain. Am.J.Hum.Genet. 22:298-303, 1970. * Petrakis, N.L., Wiesenfeld, S.L., Sams, B.J., Collen, M.F., Cutler, J.L., and Siegelaub, A.B. Prevalence of sickle-cell trait and glucose-6-phosphate dehydrogenase deficiency. N.Engl.J.Med. 282:767-770, 1970. * Reys, L., Manso, C., and Stamatoyannopoulos, G. Genetic studies on Southeastern Bantu of Mozambique. I. Variants of glucose-6-phosphate dehydrogenase. Am.J.Hum.Genet. 22:203-215, 1970. * Richardson, B.J. and Czuppon, A.B. Some properties of red blood cell glucose-6-phosphate dehydrogenase from three species of kangaroo. Aust.J.Biol.Sci. 23:1305-1306, 1970. * Rodney, G.E., Jacob, H.S., Holmes, B., McArthur, J.R., and Good, R.A. Leucocyte G.6-P.D. levels and bactericidal activity. Lancet 1:355-356, 1970. * Rosa, R., Alexandre, Y., Kaplan, J.C., and Dreyfus, J.C. Comportement immunologique de la glucose-6-phosphate-deshydrogenase erythrocytaire chez des mutants deficients. Clin.Chim.Acta 29:209-214, 1970. * Salgado, M.R.I. and Lionel, N.D.W. A comparative trial of furazolidone and chloramphenicol in thyphoid and parathyphoid fever. Ceylon Med.J. 15:159-162, 1970. Notes: Jaundice in one case. Hb? * Schlegel, R.J. and Bellanti, J.A. Leucocyte G-6-PD deficiency and bactericidal activity. Lancet 1:677, 1970. * Shahidi, N.T. and Westring, D.W. Acetylsalicylic acid-induced hemolysis and its mechanism. J.Clin.Invest. 49:1334-1340, 1970. * Snyder, L.M., Necheles, T.F., and Reddy, W.J. G-6-PD Worcester: A new variant, associated with x-linked optic atrophy. Am.J.Med. 49:125-132, 1970. * Staal, G.E.J., Punt, K., Geerdink, R.A., Bos, C.C., and Bartstra, H. A possible new variant of G-6-PD with decreased activity (G-6-PD Utrecht) in a Dutch family with hereditary spherocytosis. Scand.J.Haematol. 7:401-403, 1970. * Stamatoyannopoulos, G., Kotsakis, P., Voigtlander, V., and Motulsky, A.G. Electrophoretic diversity of glucose-6-phosphate dehydrogenase among Greeks. Am.J.Hum.Genet. 22:587-596, 1970. * Stamatoyannopoulos, G., Voigtlaender, V., and Akrivakis, A. Thessaly variant of glucose-6-phosphate dehydrogenase. Humangenetik 9:23-25, 1970. * Steele, M.W. Incomplete dosage compensation for glucose-6-phosphate dehydrogenase in human embryos and newborns. Nature 227:496-498, 1970. * Teunis, B.S., Leftwich, E.I., and Pierce, L.E. Acute methemoglobinemia and hemolytic anemia due to toluidine blue. Arch.Surg. 101:527-531, 1970. * Waitz, R., Boivin, P., Oberling, F., Casenave, J.P., North, M.L., and Mayer, S. Variante gd (-) Strasbourg de la

glucose-6-phosphate-dehydrogenase. Nouv.Rev.Fr.Hematol. 10:312-314, 1970. * Weitkamp, L. and Neel, J.V. Gene frequencies and microdifferentiation among the Makiritare Indians. 3. Nine erythrocyte enzyme systems. Am.J.Hum.Genet. 22:533-537, 1970. * Wiesenfeld, S.L., Petrakis, N.L., Sams, B.J., Collen, M.F., and Cutler, J.L. Elevated blood pressure, pulse rate and serum creatinine in negro males deficient in glucose-6-phosphate dehydrogenase. N.Engl.J.Med. 282:1001-1002, 1970. * Yeung, C.Y., Lai, H.C., and Leung, N.K. Fluorescent spot test for screening erythrocyte glucose-6-phosphate dehydrogenase deficiency in newborn babies. J.Pediatr. 76:931-934, 1970. * Yoshida, A. Enzyme purification by selective elution with substrate analog from ion-exchange columns: Application to glucose-6-phosphate dehydrogenase, pseudocholinesterase, lactate dehydrogenase, and alanine dehydrogenase. Anal.Biochem. 37:357-367, 1970. * Yoshida, A. Amino acid substitution (histidine to tyrosine) in a glucose-6-phosphate dehydrogenase variant (G6PD Hektoen) associated with overproduction. J.Mol.Biol. 52:483-490, 1970. * Yoshida, A., Baur, E.W., and Motulsky, A.G. A Philipino glucose-6-phosphate dehydrogenase variant (G6PD Union) with enzyme deficiency and altered substrate specificity. Blood 35:506-513, 1970. * Yoshida, A. and Hoagland, V.D.J. Active molecular unit and NADP content of human glucose-6-phosphate dehydrogenase. Biochem.Biophys.Res.Commun. 40:1167-1172, 1970. * Afolayan, A. and Luzzatto, L. Genetic variants of human erythrocyte glucose-6-phosphate dehydrogenase. I. Regulation of activity by oxidized and reduced nicotinamide adenine dinucleotide phosphate. Biochemistry 10:415-419, 1971. * Arends, T. Hemoglobinopathies and enzyme deficiencies in Latin American populations. In: The Ongoing Evolution of Latin American Populations,Anonymous Springfield, Ill.Charles C. Thomas, 1971, * Baehner, R.L., Nathan, D.G., and Castle, W.B. Oxidant injury of caucasian glucose-6-phosphate dehydrogenase-deficient red blood cells by phagocytosing leukocytes during infection. J.Clin.Invest. 50:2466-2473, 1971. * Benhr, H.C., Waller, H.D., Arnold, H., Blume, K.G., and Lhr, G.W. Glucose-6-P-dehydrogenase Typ Bodensee (eine neue Enzymvariante). Klin.Wochenschr. 49:1058-1062, 1971. * Benhr, H.C., Klumpp, F., and Waller, H.D. Glucose-6-phosphate dehydrogenase Typ Schwaben. Dtsch.Med.Wochenschr. 96:1029-1032, 1971. * Bonsignore, A., Cancedda, R., Nicolini, A., Damiani, G., and De Flora, A. Metabolism of human erythrocyte glucose-6-phosphate dehydrogenase VI. Interconversion of multiple molecular forms. Arch.Biochem.Biophys. 147:493-501, 1971. * Bonsignore, A., Lorenzoni, I., Cancedda, R., Cosulich, M.E., and De Flora, A. Effect of divalent cations on the structure of human erythrocyte glucose-6-P dehydrogenase. Biochem.Biophys.Res.Commun. 42:159-165, 1971. * Buchanan, N., Cassel, R., and Jenkins, T. G-6-PD deficiency and piperazine. BMJ 2:110, 1971. * Chan, T.K., Chesterman, C.N., McFadzean, A.J.S., and Todd, D. The survival of glucose-6-phosphate dehydrogenase-deficient erythrocytes in patients with typhoid fever on chloramphenicol therapy. J.Lab.Clin.Med. 77:177-184, 1971. * Chan, T.K. and Lai, M.C.S. Double hererozygosity for

glucose-6-phosphate dehydrogenase deficiency. J.Med.Genet. 8:149-152, 1971. * Corrias, L. and Melis, L. Carenza eritrocitaria di G-6-PD nei donatori di snague di oristano. Quad.Sclavo.Diagn. 7:595-599, 1971. * Cotton, D.W.K. and Sutorius, A.H.M. Inhibiting effect of some antimalarial substances on glucose-6-phosphate dehydrogenase. Nature 233:197, 1971. * Fialkow, P.J., Sagebiel, R.W., Gartler, S.M., and Rimoin, D.L. Multiple cell origin of hereditary neurofibromas. N.Engl.J.Med. 284:298-300, 1971. * Gray, G.R. and Marion, R.B. Thalassemia and G-6-PD deficiency in Chinese-Canadians: Admission screening of a hospital population. Can.Med.Assoc.J. 105:283-286, 1971. * Heinrich, R.A., Smith, T.C., and Buchanan, R.A. A pharmacological study of a new sulfonamide in glucose-6-phosphate dehydrogenase deficient subjects. J.Clin.Pharmacol. 11:428-432, 1971. * Hutton, J.J. Genetic regulation of glucose 6-phosphate dehydrogenase activity in the inbred mouse. Biochem.Genet. 5:315-331, 1971. * Kahn, A., Boivin, P., Hakim, J., and Lagneau, J. Heterogeneite des glucose-6-phosphate deshydrogenase erythrocytaire deficitaires dans la race noire. Etude cinetique et description de deux nouvelles variantes Gd (-) Dakar et Gd (-) Mali. Nouv.Rev.Fr.Hematol. 11:741-758, 1971. * Kwiatkowska, J. and Kacprzak-Bergman, I. New erythrocyte glucose-6-phosphate dehydrogenase variant. Acta Haematol.(Basel) 46:188-192, 1971. * Livingstone, F.B. Malaria and human polymorphisms. Annu.Rev.Genet. 5:33-64, 1971. * Lopez, R. and Cooperman, J.M. Glucose-6-phosphate dehydrogenase deficiency and hyperbilirubinemia in the newborn. Am.J.Dis.Child. 122:66-70, 1971. * Luzzatto, L. and Afolayan, A. Genetic variants of human erythrocyte glucose-6-phosphate dehydrogenase. II. In vitro and in vivo function of the A-variant. Biochemistry 10:420-423, 1971. * McCaffrey, R.P., Halsted, C.H., Wahab, M.F.A., and Robertson, R.P. Chloramphenicol-induced hemolysis in caucasian glucose-6-phosphate dehydrogenase deficiency. Ann.Intern.Med. 74:722-726, 1971. * Moeller, N.P.H. and Steensgaard, J. Studies on the glutathione stability of normal and glucose-6-phosphate-deficient human erythrocytes. Scand.J.Clin.Lab.Invest. 28:277-282, 1971. * Motulsky, A.G., Yoshida, A., and Stamatoyannopoulos, G. Variants of glucose-6-phosphate dehydrogenase. Ann.NY Acad.Sci. 179:636-643, 1971. * Murray, R.F., Hobbs, J., and Payne, B. Possible clonal origin of common warts (verruca vulgaris). Nature 232:51-52, 1971. * Naik, S.N. and Anderson, D.E. The association between glucose-6-phosphate dehydrogenase deficiency and cancer in American negroes. Oncology 25:356-364, 1971. * Naik, S.N. and Anderson, D.E. Glucose-6-phosphate dehydrogenase and hemoglobin types in cattle. J.Anim.Sci. 32:132-136, 1971. * Necheles, T.F., Snyder, L.M., and Strauss, W. Glucose-6-phosphate dehydrogenase Boston. A new variant associated with congenital nonspherocytic hemolytic disease. Humangenetik 13:218-221, 1971.

* Perkins, R.P. Hydrops fetalis and stillbirth in a male glucose-6-phosphate dehydrogenase- deficient fetus possibly due to maternal ingestion of sulfisoxazole. Am.J.Obstet.Gynecol. 111:379-381, 1971. * Richardson, B.J., Czuppon, A.B., and Sharman, G.B. Inheritance of glucose-6-phosphate dehydrogenase variation in kangaroos. Nature (New Biol.) 230:154-155, 1971. * Rosen, P.J., Johnson, C., McGehee, W.G., and Beutler, E. Failure of methylene blue treatment in toxic methemoglobinemia. Association with glucose-6-phosphate dehydrogenase deficiency. Ann.Intern.Med. 75:83-86, 1971. Notes: (B276). * Rosenberg, P.H. Decrease in reduced glutathione and NADPH and inhibition of glucose-6- phosphate dehydrogenase activity caused by metabolites of fluroxene and halothane. Ann.Med.Exp.Biol.Fenn. 49:81-88, 1971. * Saha, N. and Banerjee, B. Erythrocyte G-6-PD deficiency among Chinese and malays of Singapore. Trop.Geogr.Med. 23:141-144, 1971. * Schrter, W., Brittinger, G., Zimmerschmitt, E., Koenig, E., and Schrader, D. Combined glucosephosphate isomerase and glucose-6-phosphate dehydrogenase deficiency of the erythrocytes: A new haemolytic syndrome. Br.J.Haematol. 20:249-261, 1971. * Sherwood, W.C., Martinez, J., and Flegel, E. Phenobarbitone: Absence of effect on erythrocyte-G-6-PD. Lancet 1:1075, 1971. * Siegel, N.H. and Beutler, E. Hemolytic anemia caused by G-6-PD Carswell, a new variant. Ann.Intern.Med. 75:437-439, 1971. Notes: (B281). * Smith, J.E. and Anwer, M.S. Studies on glucose-6-phosphate dehydrogenase:Variability in ATP inhibition. Experientia 27:835-836, 1971. * Smith, J.E. A modified screening method for estimating erythrocyte glucose-6-phosphate dehydrogenase. Res.Vet.Sci. 12:198-199, 1971. * Smith, J.W., Townsend, D.E., and Sparkes, R.S. Genetic variants of glucose-6-phosphate dehydrogenase in the study of carcinoma of the cervix. Cancer 28:529-532, 1971. * Smith, J.W., Townsend, D.E., and Sparkes, R.S. Glucose-6-phosphate dehydrogenase polymorphism: A valuable tool to study tumor origin. Clin.Genet. 2:160-162, 1971. * Spirer, Z., Binor, Z., and Bogair, N. G.-6-P.D. and childhood infection. Lancet 2:661-662, 1971. * Stamatoyannopoulos, G., Voigtlander, V., Kotsakis, P., and Akrivakis, A. Genetic diversity of the "Mediterranean" glucose-6-phosphate dehydrogenase deficiency phenotype. J.Clin.Invest. 50:1253-1261, 1971. * Stocks, J., Kemp, M., and Dormandy, T.L. Increased susceptibility of red-blood-cell lipids to autooxidation in haemolytic states. Lancet 1:266-269, 1971. * Streiff, F. and Vigneron, C. Chronic haemolytic anemia due to a defect of glucose-6-phosphate dehydrogenase (G6PD) in a Lorraine family. Demonstration of a new type of the enzyme: Gd(-) Nancy. Nouv.Rev.Fr.Hematol. 11:279-290, 1971. * Wang, Y.M., Patterson, H.J., and Van Eys, J. The potential use of xylitol in glucose-6-phosphate dehydrogenase deficiency anemia. J.Clin.Invest. 50:1421-1428, 1971. * Welt, S.I., Jackson, E.H., Kirkman, H.N., and Parker, J.C. The effects of certain drugs on the hexose monophosphate shunt of human red cells. Ann.NY Acad.Sci. 179:625-635, 1971. * Yoshida, A., Beutler, E., and Motulsky, A.G. Table of human

glucose-6-phosphate dehydrogenase variants. Bull.WHO 45:243-253, 1971. Notes: (B295). * Yoshida, A., Watanabe, S., and Gartler, S.M. Identification of HeLa cell glucose 6-phosphate dehydrogenase. Biochem.Genet. 5:533-539, 1971. * Youel, D.B., Strickland, G.T., Binh, B.A., Clarkson, R., and Blackwell, R.Q. Low incidence of erythrocyte G-6-PD deficiency in Vietnamese and Montagnards of South Vietnam. Vox Sang. 20:555-558, 1971. * Allen, S.D.,Jr. and Wilkerson, J.L. The importance of glucose-6-phosphate dehydrogenase screening in a urologic practice. J.Urol. 107:304-305, 1972. * Allesio, L. and Morselli, G. Occupational exposure to nalidixic acid. BMJ 4:110-111, 1972. * Angle, C.R. Glucose-6-phosphate dehydrogenase deficiency and acute renal failure. Lancet 2:134, 1972. * Babalola, O., Cancedda, R., and Luzzatto, L. Genetic variants of glucose 6-phosphate dehydrogenase from human erythrocytes: Unique properties of the A- variant isolated from "deficient" cells. Proc.Natl.Acad.Sci.USA 69:946-950, 1972. * Bakay, B., Nyhan, W.L., and St.J.Monkus, E. Change in electrophoretic mobility of glucose-6-phosphate dehydrogenase with aging of erthrocytes. Pediatr.Res. 6:705-712, 1972. * Bakshi, S. and Singh, J. Acute haemolytic anaemia in typhoid fever. Indian J.Pediatr. 39:270-273, 1972. * Beutler, E. Glucose 6-phosphate dehydrogenase deficiency. In: Hematology, edited by Williams, W.J., Beutler, E., Erslev, A.J., and Rundles, R.W.New York:McGraw-Hill, Inc. 1972,p. 391-399. Notes: (B322F). * Beutler, E., Grooms, A.M., Morgan, S.K., and Trinidad, F. Chronic severe hemolytic anemia due to G-6-PD Charleston: A new deficient variant. J.Pediatr. 80:1005-1009, 1972. Notes: (B301). * Beutler, E. Glucose-6-phosphate dehydrogenase deficiency. In: The Metabolic Basis of Inherited Disease, edited by Stanbury, J.B., Wyngaarden, J.B., and Fredrickson, D.S.New York:McGraw-Hill, Inc. 1972,p. 1358-1388. Notes: (B294). * Beutler, E. Red cell metabolism. A. Defects not causing hemolytic disease. B. Environmental modification. Biochim.Biophys.Acta 54:759-764, 1972. Notes: (B314). * Beutler, E. Drug-induced anemia. Fed.Proc. 31:141-146, 1972. Notes: (B290). * Bienzle, U., Lucas, A.O., Ayeni, O., and Luzzatto, L. Glucose-6-phosphate dehydrogenase and malaria. Greater resistance of females heterozygous for enzyme deficiency and of males with non-deficient variant. Lancet 1:107-110, 1972. * Bonsignore, A. and De Flora, A. Regulatory properties of glucose-6-phosphate dehydrogenase. Curr.Top.Cell Regul. 6:21-62, 1972. * Brown, C.B., McMillan, J.M., Bateman, C.J.T., and Cattell, W.R. Acute renal failure following analgesic overdose in G6PD deficiency. Br.J.Urol. 44:155-160, 1972. * Chan, T.K. G-6-PD deficiency, typhoid, and co-trimoxazole. Lancet 2:1258, 1972. * Chan, T.K. and Todd, D. Characteristics and distribution of glucose-6-phosphate dehydrogenase-deficient variants in South

China. Am.J.Hum.Genet. 24:475-484, 1972. * Chan, T.K., Todd, D., and Lai, M.C.S. Glucose 6-phosphate dehydrogenase: Identity of erythrocyte and leukocyte enzyme with report of a new variant in Chinese. Biochem.Genet. 6:119-124, 1972. * Cooper, M.R., DeChatelet, L.R., McCall, C.E., La Via, J.F., Spurr, C.L., and Baehner, R.L. Complete deficiency of leukocyte glucose-6-phosphate dehydrogenase with defective bactericidal activity. J.Clin.Invest. 51:769-778, 1972. * De Laurenzi, A., Papa, G., Amadori, S., Fontana, L., and Monarca, B. Anemia emolitica acuta in soggetto affetto da favismo ittero-emoglobinurico dopo assunzione di un farmaco antitussigeno. Haematologica (Pavia) 57:90-94, 1972. * Ellis, N. and Alperin, J.B. Laboratory suggestions: A rapid method for electrophoresis of erythrocyte glucose-6-phosphate dehydrogenase on cellulose acetate plates. Am.J.Clin.Pathol. 57:534-536, 1972. * Erickson, R.P., Stites, D.P., Fudenberg, H.H., and Epstein, C.J. Altered levels of glucose-6-phosphate dehydrogenase stabilizing factors in X-linked chronic granulomatous disease. J.Lab.Clin.Med. 80:644-653, 1972. * Fialkow, P.J., Martin, G.M., Klein, G., Clifford, P., and Singh, S. Evidence for a clonal origin of head and neck tumors. Int.J.Cancer 9:133-142, 1972. * Gellady, A. and Greenwood, R.D. G-6-PD hemolytic anemia complicating diabetic ketoacidosis. J.Pediatr. 80:1037-1038, 1972. * Gibbs, W.N., Ottey, F., and Dyer, H. Distribution of glucose-6-phosphate dehydrogenase phenotypes in Jamaica. Am.J.Hum.Genet. 24:18-23, 1972. * Hakim, S.M.A., Baxi, A.J., Balakrishnan, V., Kulkarni, K.V., Rao, S.S., and Jhala, H.I. Glucose-6-phosphate dehydrogenase deficiency and colour-vision studies in Indian muslims. Humangenetik 15:90-92, 1972. * Haltalin, K.C. and Nelson, J.D. Failure of furazolidone therapy in shigellosis. Am.J.Dis.Child. 123:40-44, 1972. * Hilgertova, J., Strakova, M., Vvrbova, H., Gregorova, I., Sonka, J., and Josifko, M. Seasonal variations of human erythrocyte glucose-6-phosphate dehydrogenase activity in relation to temperature and dehydroepiandrosterone excretion. Clin.Chim.Acta 36:511-515, 1972. * Howell, E.B., Nelson, A.J., and Jones, O.W. A new G-6-PD variant associated with chronic non-spherocytic haemolytic anaemia in a negro family. J.Med.Genet. 9:160-164, 1972. * Kahn, A., Lagneau, J., Boivin, P., and Hakim, J. Importance et role des groupes imidazole et sulfhydrile dans l'activite catalytique de la glucose 6 phosphate deshydrogenase erythrocytaire humaine. Biochim.Biophys.Acta 54:997-1004, 1972. * Kahn, A., Boivin, P., and Lagneau, J. Etude cinetique et thermodynamique de la glucose-6-phosphate-deshydrogenase erythrocytaire chez l'homme. Application a 7 variantes differentes de la race noire. Biochim.Biophys.Acta 54:775-785, 1972. * Khan, P.M., Van Someren, H., De Jong, W.W., and Vervloet, M. Red cell enzme polymorphisms in rhesus monkeys and chimpanzees. Transplant.Proc. 4:137-140, 1972. * Kojima, H. Congenital nonspherocytic hemolytic disease (CNHD) due to a G-6-PD variant: G-6-PD Kyoto. Acta Haematol.Jpn. 35:32-38, 1972. * Larcan, A., Kaiffer, M., Maitrehanche, M., Genetet, B., and

Vigneron, C. Insuffisance renale aigue. Revelatrice d'un deficit en glucose-6-phosphate deshydrogenase: Gravite de l'hemolyse istrogene. Nouv.Presse Med. 35:2299-2304, 1972. * Lisker, R., Linares, C., and Motulsky, A.G. Glucose-6-phosphate dehydrogenase Mexico. A new variant with enzyme deficiency, abnormal mobility and absence of hemolysis. J.Lab.Clin.Med. 79:788-793, 1972. * Lowe, M.L., Stella, A.F., Mosher, B.S., Gin, J.B., and Demetriou, J.A. Microfluorometry of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in red cells. Clin.Chem. 18:440-445, 1972. * McCaffrey, R.P., Farid, Z., and Kent, D.C. Acute haemolysis with ambilhar treatment in glucose-6-phosphate dehydrogenase deficiency. Trans.R.Soc.Trop.Med.Hyg. 66:795-797, 1972. * McCurdy, P.R., Schneer, J.H., and Hansen, I.M. Red cell glucose-6-phosphate dehydrogenase variants in Rumania. Rev.Europ.Etudes Clin.Biol. 17:66-69, 1972. * McIntire, M.S. and Angle, C.R. Air lead: Relation to lead in blood of black school children deficient in glucose-6-phosphate dehydrogenase. Science 177:520-522, 1972. * Meloni, T., Dorf, A., and Cutillo, S. Effect of barbituric acid on hyperbilirubinemia in newborn infants with glucosephosphate dehydrogenase deficiency in the erythrocytes. Helv.Paediatr.Acta 27:197-202, 1972. * Metzger, R.P., Metzger, S.A., and Parsons, R.L. A study of glucose and xylose oxidation catalyzed by the glucose-6-phosphate dehydrogenase of rat liver cytosol. Arch.Biochem.Biophys. 149:102-109, 1972. * Millar, J., Peloquin, R., and De Leeuw, N.K.M. Phenacetin-induced hemolytic anemia. Can.Med.Assoc.J. 106:770-775, 1972. * Othieno-Obel, A. East African variant of glucose-6-phosphate dehydrogenase. East Afr.Med.J. 49:230-234, 1972. * Owusa, S.K. Absence of glucose-6-phosphate dehydrogenase in red cells of an African. BMJ 4:25-26, 1972. * Owusu, S.K., Foli, A.K., Konotey-Ahulu, F.I.D., and Janosi, M. Frequency of glucose-6-phosphate dehydrogenase deficiency in typhoid fever in Ghana. Lancet 1:320, 1972. * Owusu, S.K. Acute haemolysis complicating co-trimoxazole therapy for typhoid fever in a patient with g.-6-P.D. Deficiency. Lancet 2:819-LETTER, 1972. * Owusu, S.K., Foli, A.K., Konotey-Ahulu, F.I.D., Addy, J.H., Janosi, M., and Larbi, E.B. Acute reversible renal failure associated with glucose-6-phosphate dehydrogenase deficiency. Lancet 1:1255-1257, 1972. * Panich, V., Sungnate, T., and Na-Nakorn, S. Acute intravascular hemolysis and renal failure in a new glucose-6phosphate dehydrogenase variant: G-6-PD Siriraj. J.Med.Assoc.Thai. 55:726-731, 1972. * Panich, V., Sungnate, T., Wasi, P., and Na-Nakorn, S. G-6-PD Mahidol. The most common glucose-6-phosphate dehydrogenase variant in Thailand. J.Med.Assoc.Thai. 55:576-585, 1972. * Paniker, N.V. and Beutler, E. Glucose-6-phosphate dehydrogenase and NADPH diaphorase in cattle erythrocytes. J.Anim.Sci. 34:75-76, 1972. Notes: (B292). * Penton, E., Pascual, C., Llanes, A., and Thielmann, K. The activity of glucose-6-phosphate dehydrogenase in whole blood samples dried and stored on filter paper. Acta Biol.Med.Ger. 28:177-180, 1972.

* Piomelli, S., Reindorf, C.A., Arzanian, M.T., and Corash, L.M. Clinical and biochemical interactions of glucose-6-phosphate dehydrogenase deficiency and sickle-cell anemia. N.Engl.J.Med. 287:213-217, 1972. * Rainer, H., Moser, K., and Honetz, N. Eine neue enzymvariante des glucose-6-phosphat-dehydrogenasemangels. In: Fortschritte der Klinischen Chemie Ensyme und Hormone, edited by Kaiser, E.Vienna:Verlag der Wiener Medizinische Akademie, 1972,p. 221-225. * Ringelhahn, B. A simple laboratory procedure for the recognition of A- (African type) G6PD deficiency in acute haemolytic crisis. Clin.Chim.Acta 36:272-274, 1972. * Rozenszajn, L.A., Shoham, D., and Menashi, T. Evaluation of glucose-6-phosphate dehydrogenase in single erythrocytes in human blood smears. Acta Haematol.(Basel) 47:303-310, 1972. * Salvidio, E., Pannacciulli, I., Ajmar, F., Garre, C., Gaetani, G., Ghio, R., Molinino, M., and Ravazzolo, R. Glucose-6-phosphatdehydrogenase-defekt der erythrozyten und favismus. In: Haemolyse Haemolytische Erkrankungen, edited by Nowicki, L., Martin, H., and Schubert, J.C.F.Munich:Lehmanns Verlag, 1972,p. 147-154. * Salvidio, E., Pannacciulli, I., Ajmar, F., Gaetani, G., Ghio, R., Molinino, M., and Garre, C. Hemolytic side effects of some antimalarial drugs. Basic Res.Malaria 39:83-100, 1972. * Srivastava, S.K., Blume, K.G., Beutler, E., and Yoshida, A. Immunological difference between glucose-6-P dehydrogenase and hexose-6-P dehydrogenase from human liver. Nature (New Biol.) 238:240-241, 1972. Notes: (B325). * Sulis, E. G-6-PD deficiency and cancer. Lancet 1:1185, 1972. * Tunail, N. and Schlegel, H.G. Phosphoenolpyruvate, a new inhibitor of glucose-6-phosphate dehydrogenase. Biochem.Biophys.Res.Commun. 49:1554-1560, 1972. * Weitkamp, L.R. and Neel, J.V. The genetic structure of a tribal population, the Yanomama Indians. IV. Eleven erythrocyte enzymes and summary of protein variants. Ann.Hum.Genet. 35:433-444, 1972. * White, P.A. Special modifications of the fluorescent screening test for glucose 6 phosphate dehydrogenase deficiency. Aust.J.Med.Technol. 3:133-136, 1972. * Witt, I. and Yoshioka, S. Biochemical characterization of a glucose-6-phosphate dehydrogenase variant with favism: G-6-PD Zaehringen. Klin.Wochenschr. 50:205-209, 1972. * Wrigley, N.G., Heather, J.V., Bonsignore, A., and De Flora, A. Human erythrocyte glucose 6-phosphate dehydrogenase: Electron microscope studies on structure and interconversion of tetramers, dimers and monomers. J.Mol.Biol. 68:483-499, 1972. * Acquaye, C.T.A. and Oldham, J.H. Variants of haemoglobin and glucose-6-phosphate dehydrogenase 1. Distribution in Southern Ghana. Ghana Med.J. 12:412-418, 1973. * Alperin, J.B. and Mills, G.C. New variants of glucose-6-phosphate dehydrogenase: G6PD Kilgore and G6PD Galveston. Tex.Rep.Biol.Med. 31:727-744, 1973. * Balinsky, D., Cayanis, E., Carter, G., Jenkins, T., and Bersohn, I. A new variant of human erythrocyte glucose-6-phosphate dehydrogenase: G6PD Port Elizabeth. Int.J.Biochem. 4:235-244, 1973. * Balinsky, D., Gomperts, E., Cayanis, E., Jenkins, T., Bryer, D., Bersohn, I., and Metz, J. Glucose-6-phosphate dehydrogenase Johannesburg: A new variant with reduced activity in a patient

with congenital non-spherocytic haemolytic anaemia. Br.J.Haematol. 25:385-391, 1973. * Barr, R.D. and Fialkow, P.J. Clonal origin of chronic myelocytic leukemia. N.Engl.J.Med. 289:307-9, 1973. * Ben-Bassat, I. and Beutler, E. Inhibition by ATP of erythrocyte glucose-6-phosphate dehydrogenase variants. Proc.Soc.Exp.Biol.Med. 142:410-411, 1973. Notes: (B332). * Benditt, E.P. and Benditt, J.M. Evidence for a monoclonal origin of human atherosclerotic plaques. Proc.Natl.Acad.Sci.USA 70:1753-1756, 1973. * Beni, A., Fioritoni, G., Salvati, A.M., Tentori, L., and Torlontano, G. Quantitation of the ultraviolet light test for erythrocyte glucose 6-phosphate. Clin.Chim.Acta 49:41-48, 1973. * Beutler, E. and Yoshida, A. Human glucose-6-phosphate dehydrogenase variants: A supplementary tabulation. Ann.Hum.Genet. 37:151-155, 1973. Notes: (B364). * Beutler, E. Screening for glucose-6-phosphate dehydrogenase deficiency. Isr.J.Med.Sci. 9:1350-1352, 1973. Notes: (B370). * Blinov, M.N., Rodriges, N., and Sanches-Perovani, K.H. Incidence of carriage of glucoso-6-phosphate-dehydrogenase deficiency of erythrocytes in the population of North Oriente province (republic of Cuba). Probl.Gematol.Pereliv.Krovi. 18:26-29, 1973. * Blume, K.G., Srivastava, S.K., Beutler, E., and Yoshida, A. Biochemische und immunologische Unterschiede zwischen Glucose-6-phosphat-dehydrogenase und Hexose-6-phosphat-dehydrogenase aus menschlicher Leber. Hoppe-Seyler's Z.Physiol.Chem. 354:213, 1973. Notes: (B339). * Buchanan, J.G., Wilson, F.S., and Nixon, A.D. Survey for erythrocyte glucose-6-phosphate dehydrogenase deficiency in Fiji. Am.J.Hum.Genet. 25:36-41, 1973. * Butler, T. G-6-PD deficiency and malaria in black Americans in Vietnam. Milit.Med. 138:153-155, 1973. * Cassimos, C., Sklavunu-Tsuruktosglu, S., Catriu, D., and Panajiotidu, C. The incidence of G 6 PD disturbances in cancer patients. IRCS (73-3) 27-2-2, 1973. * Cohen, P.T.W., Omenn, G.S., Motulsky, A.G., Chen, S.-H., and Giblett, E.R. Restricted variation in the glycolytic enzymes of human brain and erythrocytes. Nature (New Biol.) 241:229-233, 1973. * Constantopoulos, A., Economopoulos, P., and Kandylas, J. Fulminant diarrhea and acute hemolysis due to g.-6-P.D. Deficiency in salmonellosis. Lancet 1:1522, 1973. * Conte, J., Durand, D., Ton-That, H., and Suc, J.M. Acute renal failure and hemolytic anemia due to red cell G6PD deficiency first manifested after chloroquine administration. J.Urol. 79:756-763, 1973. * Crookston, J.H., Yoshida, A., Lin, M., and Booser, D.J. G 6 PD Toronto. Biochem.J. 8:259-265, 1973. * De Flora, A., Giuliano, F., and Morelli, A. Rapid purification of glucose 6-phosphate dehydrogenase from human erythrocytes by means of affinity chromatography. Ital.J.Biochem. 22:258-270, 1973. * Dickson, L.G., Johnson, C.B., and Johnson, D.R. Automated fluorometric method for screening for erythrocyte glucose-6phosphate dehydrogenase deficiency. Clin.Chem. 19:301-303, 1973.

* Dimopoulos, C., Morakis, A., Dimopoulos, B., Zervas, A., Panayiotides, N., and Doutsias, A. Anemie hemolytique aigue consecutive a l'administration de nitrofurane et de novalgine chez deux malades presentant un deficit en glucose 6-phosphate-dehydrogenase erythrocytaire. J.Urol.(Paris) 79:524-528, 1973. * Ermilchenko, G.V. and Solovieva, N.P. A study of the incidence of deficiency of the activity of glucoso-6- phosphoric dehydrogenase in the blood of persons residing in the Arkhangelsk region. Probl.Gematol.Pereliv.Krovi. 18:23-26, 1973. * Fialkow, P.J., Klein, E., Klein, G., Clifford, P., and Singh, S. Immunoglobulin and glucose-6-phosphate dehydrogenase as markers of cellular origin in Burkitt lymphoma. J.Exp.Med. 138:89-102, 1973. * Frischer, H., Carson, P.E., Bowman, J.E., and Rieckmann, K.H. Visual test for erythrocytic glucose-6-phosphate dehydrogenase, 6-phosphogluconic dehydrogenase, and glutathione reductase deficiencies. J.Lab.Clin.Med. 81:613-624, 1973. * Frischer, H., Bowman, J.E., Carson, P.E., Rieckmann, K.H., Willerson, D.J., and Colwell, E.J. Erythrocytic glutathione reductase, glucose-6-phosphate dehydrogenase, and 6-phosphogluconic dehydrogenase deficiencies in populations of the United States, South Vietnam, Iran, and Ethiopia. J.Lab.Clin.Med. 81:603-612, 1973. * Gaetani, G.F., Garre, C.S., Ajmar, F., and Bianchi, G.L. Influence of riboflavin and of erythrocyte stroma on glutathione reductase activity in normal, glucose 6 phosphate dehydrogenase deficient and low glutathione reductase individuals. Biomedicine 19:469-474, 1973. * Geerdink, R.A., Horst, R., and Staal, G.E.J. An Iraqi Jewish family with a new red cell glucose-6-phosphate dehydrogenase variant (Gd-Bagdad) and kernicterus. Isr.J.Med.Sci. 9:1040-1043, 1973. * Glader, B.E. and Conrad, M.E. Hemolysis by diphenylsulfones: Comparative effects of DDS and hydroxylamine-DDS. J.Lab.Clin.Med. 81:267-272, 1973. * Glass, L., Rajegowda, B.K., Bowen, E., and Evans, H.E. Exposure to quinine and jaundice in a glucose-6-phosphate dehydrogenase-deficient newborn infant. J.Pediatr. 82:734-735, 1973. * Gray, G.R., Klebanoff, S.J., Stamatoyannopoulos, G., Austin, T., Naiman, S.C., Yoshida, A., Kliman, M.R., and Robinson, G.C.F. Neutrophil dysfunction, chronic granulomatous disease, and nonspherocytic haemolytic anaemia caused by complete deficiency of glucose-6-phosphate dehydrogenase. Lancet 2:530-534, 1973. * Grech, J.L. and Vicatou, M. Glucose-6-phosphate dehydrogenase deficiency in Maltese newborn infants. Br.J.Haematol. 25:261-269, 1973. * Hartz, J., El-Maghrabi, R., Namen, A., Gabr, M., Bowman, J., Carson, P., Ajmar, F., and Kamel, K. Enzyme studies in G-6-PD deficient erythrocytes from Egyptians, italians, and American negroes (pyrophosphatase, 6-PGD, glutamic-oxalacetic transaminase, acid phosphatase, catalase and superoxide dismutase assays). Clin.Chim.Acta 48:117-126, 1973. * Idelson, L.I., Rustamov, R.S.H., Lysenko, A.I.A., Abrashkin-Zhuchkov, R.G., and Gorbunova, I.U.P. Attempt at preventing the hemolytic action of primaquine in persons with a glucose-6-phosphate dehydrogenase activity deficit in the erythrocytes by the simultaneous administration of xylitol and riboflavin. Probl.Gematol.Pereliv.Krovi. 18:24-28, 1973.

* Kahn, A., Leger, J., Boivin, P., Hollard, D., and Hakim, J. Anemie hemolytique congenitale non spherocytaire par deficit en G 6 PD: Etude physiologique et biocheimique d'une variante inhabituelle. Rapport avec la G-6-PD "Benevento". Biochim.Biophys.Acta 55:1121-1128, 1973. * Kahn, A., Boivin, P., and Lagneau, J. Phenotypes of erythrocytic glucose-6-phosphate dehydrogenase among black people. Humangenetik 18:261-270, 1973. * Karayalcin, G., Kim, K.Y., Aballi, A.J., and Lanzkowsky, P. Glucose-6-phosphate dehydrogenase (G-6-PD) deficiency and hyperbilirubinemia in Black American term infants. American Society of Hematology Abstract 165:92, 1973. (Abstract) * Lewis, R.A. Glucose-6-phosphate dehydrogenase electrophoresis in Ghanaians with AA and SS haemoglobin. Acta Haematol.(Basel) 50:105-111, 1973. * Luzzatto, L. New developments in glucose-6-phosphate dehydrogenase deficiency. Isr.J.Med.Sci. 9:1484-1498, 1973. * Luzzatto, L. Studies of polymorphic traits for the characterization of populations. African populations South of the Sahara. Isr.J.Med.Sci. 9:1181-1194, 1973. * Malaka-Zafiriu, K., Tsiures, I., Danielides, B., and Cassimos, C. Salicylamide glucuronide formation in newborns with severe jaundice of unknown etiology and due to glucose 6 phosphate dehydrogenase deficiency in Greece. Helv.Paediatr.Acta 28:323-329, 1973. * Marsicano, A.R.J., Hutton, J.J., and Bryant, W.M. Fatal hemolysis from mafenide treatment of burns in a patient with glucose-6-phosphate dehydrogenase deficiency. Plast.Reconstr.Surg. 52:197-199, 1973. * McCurdy, P.R., Maldonado, N., Dillon, D.E., and Conrad, M.E. Variants of glucose-6-phosphate dehydrogenase (G-6-PD) associated with G-6-PD deficiency in Puerto Ricans. J.Lab.Clin.Med. 82:432-437, 1973. * Meloni, T., Cagnazzo, G., Dore, A., and Cutillo, S. Phenobarbital for prevention of hyperbilirubinemia in glucose-6-phosphate dehydrogenase deficient newborn infants. J.Pediatr. 82:1048-1051, 1973. * Meyer, H.A. Acute haemolysis associated with typhoid fever and G-6-PD deficiency. Lancet 1:729-730, 1973. * Milbauer, B., Peled, N., and Svirsky, S. Neonatal hyperbilirubinemia and glucose-6-phosphate dehydrogenase deficiency. Isr.J.Med.Sci. 9:1547-1552, 1973. * Miwa, S. Hereditary hemolytic anemia due to erythrocyte enzyme deficiency. Acta Haematol.Jpn. 36:573-615, 1973. * Naiman, S.C., Gray, G.R., and Robinson, G. Chronic granulomatous disease associated with leukocyte and erythrocyte glucose-6-phosphate dehydrogenase (G-6-P.D.) deficiency. Ann.R.Coll.Phy.Surg.Canada 6:30, 1973. * Panich, V. The occurrence of G-6-PD Union in Thailand. Humangenetik 17:169-171, 1973. * Panich, V. Clinical pictures of acute hemolysis in G-6-PD Mahidol; report on 10 patients. J.Med.Assoc.Thai. 56:476-484, 1973. * Panich, V. and Sungnate, T. Characterization of glucose-6-phosphate dehydrogenase in Thailand. Humangenetik 18:39-46, 1973. * Piomelli, S., Corash, L., and Arzanian, M. Interactions of G6PD deficiency and sickle cell anemia. Pediatr.Res. 7:360, 1973. * Rasbridge, M.R. and Scott, G.L. The haemolytic action of Dapsone: The effect on red-cell glycolysis. Br.J.Haematol.

24:169-181, 1973. * Sanpitak, N., Supalert, Y., Chayutimonkul, L., and Flatz, G. Combined erythrocyte phosphohexose isomerase and glucose-6-phosphate dehydrogenase deficiency. Hum.Hered. 23:83-87, 1973. * Sansone, G. and Perroni, L. Variante A- della G-6-PD in un ceppo familiare di origine siciliana. Pathologica 65:81-84, 1973. * Selroos, O. and Vuopio, P. Glucose-6-phosphate dehydrogenase deficiency and myelofibrosis. Scand.J.Haematol. 11:106-111, 1973. * Singh, S. Distribution of certain polymorphic traits in populations of the Indian peninsula and South Asia. Isr.J.Med.Sci. 9:1225-1237, 1973. * Smith, J.E. and Dolberg, M. Glucose-6-phosphate dehydrogenase East Bengal: A new variant. IRCS Sept. 1973. * So, P.L., Chan, T.K., Lam, S.K., Teng, C.S., Yeung, R.T.T., and Todd, D. Cortisol metabolism in glucose-6-phosphate dehydrogenase deficiency. Metabolism 22:1443-1448, 1973. * Spissu, A., Uras, A., Devoto, G., and Iannelli, S. Porfiria acuta intermittente e carenza di G-6-PD. Descrizione di un caso. Rassegna Medica Sarda 75:307-314, 1973. * Steele, M.W. and Migeon, B.R. Sex differences in activity of glucose-6-phosphate dehydrogenase from cultured human fetal lung cells despite X-inactivation. Biochem.Genet. 9:163-168, 1973. * Szeinberg, A. and Peled, N. Detection of glucose-6-phosphate dehydrogenase deficiency in the newborn using blood specimens dried on filter paper. Isr.J.Med.Sci. 9:1353-1354, 1973. * Tugwell, P. Glucose-6-phosphate-dehydrogenase deficiency in Nigerians with jaundice associated with lobar pneumonia. Lancet 1:968-969, 1973. * Vergnes, H., Gherardi, M., Quilici, J.C., Yoshida, A., and Giacardy, R. G6PD Luz-Saint-Sauveur: A new variant with abnormal electrophoretic mobility mild enzyme deficiency and absence of haematological disorders. IRCS 3:14, 1973. * Verhorst, D. Polymorphism in glucose-6-phosphate dehydrogenase in the german large-white. Anim.Bld.Groups Biochem.Genet. 4:65-68, 1973. * Vuopio, P., Harkonen, R., Johnsson, R., and Nuutinen, M. Red cell glucose-6-phosphate dehydrogenase deficiency in Finland. Ann.Clin.Res. 5:168-173, 1973. * Waller, H.D., Luer, S., and Benhr, H.C. Stoffwechselwirkungen von Chloroquin und Primaquin in Erythrocyten. Beitrag zum Haemolysemechanismus durch Antimalariamedikamente bei Glucose-6-p-dehydrogenase-mangel. Klin.Wochenschr. 51:1185-1190, 1973. * Yoshida, A. Hemolytic anemia and G-6-PD deficiency. Science 179:532-537, 1973. * Yoshida, A. and Lin, M. Regulation of glucose-6-phosphate dehydrogenase activity in red blood cells from hemolytic and nonhemolytic variant subjects. Blood 41:877-891, 1973. * Yoshida, A. Change of activity and substrate specificity of human glucose 6-phosphate dehydrogenase by oxidation. Arch.Biochem.Biophys. 159:82-88, 1973. * Yoshida, A., Giblett, E.R., and Malcolm, L.A. Heterogeneous distribution of glucose-6-phosphate dehydrogenase variants with enzyme deficiency in the Markham valley area of New Guinea. Ann.Hum.Genet. 37:145-150, 1973. * Balinsky, D., Rootman, A.J., Nurse, G.T., Cayanis, E., Lane, A., Jenkins, T., and Bersohn, I. G6PD Kuanyama: A new variant of human erythrocyte glucose-6-phosphate dehydrogenase showing

slower than normal electrophoretic mobility. S.Afr.J.Med.Sci. 39:5-13, 1974. * Bansard-Desmidt, N. Mise en evidence de deux variantes erythrocytaires de la glucose-6- phosphate deshydrogenase chez un homme presentant un deficit enzymatique partiel. Clin.Chim.Acta 56:207-209, 1974. * Beutler, E., Johnson, C., Powars, D., and West, C. Prevalence of glucose-6-phosphate dehydrogenase deficiency in sickle cell disease. N.Engl.J.Med. 290:826-828, 1974. Notes: (B377). * Beutler, E., Matsumoto, F., and Daiber, A. Nonspherocytic hemolytic anemia due to G-6-PD Panama. IRCS 2:1389, 1974. Notes: (B386). * Brewster, M.A., Berry, D.H., and Murphey, M.N. Automated reaction rate analysis of erythrocyte glucose-6-phosphate dehydrogenase and glutathione reductase activities. Biochem.Med. 10:229-235, 1974. * Castro, G.A.M. and Snyder, L.M. G6PD San Jose: A new variant characterized by NADPH inhibition studies. Humangenetik 21:361-363, 1974. * Chan, T.K., Todd, D., and Tso, S.C. Red cell survival studies in glucose-6-phosphate dehydrogenase deficiency. Bull.Hong Kong Med.Assoc. 26:41-48, 1974. * Chan, T.K. and McFadzean, A.J.S. Haemolytic effect of trimethoprim:sulphamethoxazole in G-6-PD deficiency. Trans.R.Soc.Trop.Med.Hyg. 68:61-62, 1974. * Crosti, N. and Cagiano-Malvezzi, D. On the acrylamide disc electrophoresis pattern of human G6PD. Biochem.Genet. 11:295-300, 1974. * Cucinell, S.A., Rebert, C., and Clyde, D. Clinical pharmacology of diformyldapsone. J.Clin.Pharmacol. 14:51-57, 1974. * De Flora, A., Morelli, A., and Giuliano, F. Human erythrocyte glucose 6-phosphate dehydrogenase. Content of bound coenzyme. Biochem.Biophys.Res.Commun. 59:406-413, 1974. * De Flora, A., Morelli, A., Benatti, U., Giuliano, F., and Molinari, M.P. Human erythrocyte glucose 6-phosphate dehydrogenase. Interaction with oxidized and reduced coenzyme. Biochem.Biophys.Res.Commun. 60:999-1005, 1974. * Der Kaloustian, V.M., Idriss-Daouk, S.H., Hallal, R.T., and Awdeh, Z.L. Analysis of human erythrocyte glucose 6-phosphate dehydrogenase isozymes by isoelectric focusing in polyacrylamide gel. Biochem.Genet. 12:51-58, 1974. * Dow, P.A., Petteway, M.B., and Alperin, J.B. Simplified method for G6PD screening using blood collected on filter paper. Am.J.Pathol. 61:333-336, 1974. * Duncan, I.W., Scott, E.M., and Wright, R.C. Gene frequencies of erythocytic enzymes of Alaskan Eskimos and Athabaskan Indians. Am.J.Hum.Genet. 26:244-246, 1974. * Eggleston, L.V. and Krebs, H.A. Regulation of the pentose phosphate cycle. Biochem.J. 138:423-435, 1974. * Fialkow, P.J. The origin and development of human tumors studied with cell markers. N.Engl.J.Med. 291:26-35, 1974. * Francke, U., Bakay, B., Connor, J.D., Coldwell, J.G., and Nyhan, W.L. Linkage relationships of X-linked enzymes glucose-6-phosphate dehydrogenase and hypoxanthine guanine phosphoribosyltransferase: Recombination in female offspring of compound heterozygotes. Am.J.Hum.Genet. 26:512-522, 1974. * Gaetani, G.D., Parker, J.C., and Kirkman, H.N. Intracellular restraint: A new basis for the limitation in response to

oxidative stress in human erythrocytes containing low-activity variants of glucose-6-phosphate dehydrogenase. Proc.Natl.Acad.Sci.USA 71:3584-3587, 1974. * Gahr, M. and Schrter, W. Glucose-6-phosphate dehydrogenase (G-6-PD) Hamburg, a new variant with chronic nonspherocytic haemolytic anaemia. Eur.J.Clin.Invest. 4:187-191, 1974. * Gibbs, W.N. The methylene blue reduction test: Evaluation of a screening method for glucose-6-phosphate dehydrogenase deficiency. Am.J.Trop.Med.Hyg. 23:1197-1202, 1974. * Gray, G.R., Naiman, S.C., and Robinson, G.C.F. Platelet function and G-6-PD deficiency. Lancet 1:997, 1974. * Harkonen, M. and Vuopio, P. Red cell glucose-6-phosphate dehydrogenase deficiency in Finland. Ann.Clin.Res. 6:187-197, 1974. * Harrison, R.A.P. The detection of hexokinase, glucosephosphate isomerase and phosphoglucomutase activities in polyacrylamide gels after electrophoresis: A novel method using immobilized glucose 6-phosphate dehydrogenase. Anal.Biochem. 61:500-507, 1974. * Howard, J.K. Human erythrocyte glutathione reductase and glucose 6-phosphate dehydrogenase activities in normal subjects and in persons exposed to lead. Clin.Sci.Mol.Med. 47:515-520, 1974. * Johnson, C., Beutler, E., Powars, D., and West, C. The relationship between G-6-PD genotype and SS disease. Clin.Res. 22:178A, 1974. Notes: (B376). * Junien, C., Kaplan, J.C., Meienhofer, M.C., Maigret, P., and Sender, A. G 6 PD Baudelocque: A new unstable variant characterized in cultured fibroblasts. Enzyme 18:48-59, 1974. * Kahn, A., Hakim, J., Boivin, P., Boucherot, J., Durand, D., and Troube, H. Leucocytes et deficits en G-6-PD erythrocytaire. Nouv.Rev.Fr.Hematol. 14:291-298, 1974. * Kahn, A., Boivin, P., Vibert, M., Cottreau, D., and Dreyfus, J.-C. Post-translational modifications of human glucose-6-phosphate dehydrogenase. Biochim.Biophys.Acta 56:1395-1407, 1974. * Kahn, A., Cottreau, D., and Boivin, P. Molecular mechanism of glucose-6-phosphate dehydrogenase deficiency. Humangenetik 25:101-109, 1974. * Kahn, A. and Dreyfus, J.C. Purification of glucose-6-phosphate dehydrogenase from red blood cells and from human leukocytes. Biochim.Biophys.Acta 334:257-265, 1974. * Kahn, A., Vives-Corrons, J.L., Cottreau, D., and Boivin, P. Glucose-6-phosphate dehydrogenase slow variant with deficiency in a Spanish family. Relationship with the Gd (-) Seattle variant. Biomedicine 21:303-307, 1974. * Kahn, A., Boulard, M., Hakim, J., Schaison, G., Boivin, P., and Bernard, J. Anemie hemolytique congenitale non spherocytaire par deficit en glucose-6-phosphate-deshydrogenase erythrocytaire. Description de deux nouvelles variantes:Gd (-) Saint Louis (Paris) et Gd (-) Hayem. Nouv.Rev.Fr.Hematol. 14:587-600, 1974. * Kahn, A., Boivin, P., Leger, J., Cottreau, D., and Hollard, D. Stabilization and activation of a human glucose-6- phosphate dehydrogenase variant with enzyme deficiency by specific antibody. Biochim.Biophys.Acta 343:431-434, 1974. * Kahn, M.A., Meienhofer, M.C., Vibert, M., and Dreyfus, J.C. Vieillissement moleculaire de la glucose 6 phosphate deshydrogenase humaine. C.R.Acad.Sci.(Paris) 278:1265-1268, 1974. * Kellermeyer, R.W. Drugs and G-6-PD deficiency of red cells.

In: Drugs and Hematologic Reactions, edited by Dimitrov, N.V. and Nodine, J.H.New York:Grune & Stratton, Inc. 1974,p. 109-122. * Kwiatkowska, J., Jacyk, W., and Zatonski, W. Some properties of erythrocyte glucose-phosphate dehydrogenase in psoriatics. Arch.Dermatol.Forsch. 249:341-347, 1974. * McCurdy, P.R., Kamel, K., and Selim, O. Heterogeneity of red cell glucose-6-phosphate dehydrogenase (G-6-PD) deficiency in Egypt. J.Lab.Clin.Med. 84:673-680, 1974. * Meloni, T., Costa, S., Dore, A., and Cutillo, S. Phototherapy for neonatal hyperbilirubinemia in mature newborn infants with erythrocyte G-6-PD deficiency. J.Pediatr. 85:560-562, 1974. * Miller, D.R. and Wollman, M.R. A new variant of glucose-6-phosphate dehydrogenase deficiency hereditary hemolytic anemia, G6PD Cornell: Erythrocyte, leukocyte, and platelet studies. Blood 44:323-331, 1974. * Milner, G., Delamore, I.W., and Yoshida, A. G-6-PD Manchester: A new variant associated with chronic nonspherocytic hemolytic anemia. Blood 43:271-276, 1974. * Nakai, T. and Yoshida, A. G6PD Heian, a glucose-6-phosphate dehydrogenase variant associated with hemolytic anemia found in Japan. Clin.Chim.Acta 51:199-203, 1974. * Nowicki, L., Strobel, S., and Martin, H. ber eine neue erythrocytere Glucose-6-Phosphatdehydrogenase-Variante, Typ Frankfurt. II. Versuche zur Aufklerung einer Strukturanomalie. Klin.Wochenschr. 52:485-492, 1974. * Nowicki, L., Strobel, S., Martin, H., and Koschwitz, U. ber Eine neue erythrocytere Glucose-6-phosphatdehydrogenase-Variante, Typ Frankfurt I. Charakterisierung der Variante durch enzymkinetische Parameter. Klin.Wochenschr. 52:478-484, 1974. Notes: G6PD Frankfurt. * Panich, V. G-6-PD variants in Laotians. Hum.Hered. 24:285-290, 1974. * Panich, V. G-6-PD Intanon. A new glucose-6-phosphate dehydrogenase variant. Humangenetik 21:203-205, 1974. * Petrakis, N.L., Petrakis, S.J., Wiesenfeld, S.L., and Spanidou, E. Possible incompatibility of glucose-6-phosphate dehydrogenase deficiency and championship athletic performance. Med.Sci.Sports Exerc. 6:191-192, 1974. * Richard, F., Belhani, M., and Colonna, P. Le deficit en glucose-6-phosphate-deshydrogenase erythrocytaire chez le nouveau-ne a Alger. Nouv.Rev.Fr.Hematol. 14:453-460, 1974. * Rozenszajn, L.A. and Joseph, D. The isozyme patterns of glucose-6-phosphate dehydrogenase in blood cells, bone marrow and other human tissues. Biochim.Biophys.Acta 364:38-44, 1974. * Schwartz, J.P., Cooperberg, A.A., and Rosenberg, A. Platelet-function studies in patients with glucose-6-phosphate dehydrogenase deficiency. Br.J.Haematol. 27:273-280, 1974. * Sonnet, J., Lievens, M., Verpoorten, C., Kriekemans, J., and Eeckels, R. Sporadic G6PD deficiency with haemolytic anaemia in two children of West European ancestry. Br.J.Haematol. 28:299-310, 1974. * Sponzo, R.W., Arseneau, J.C., and Canellos, G.P. Procarbazine induced oxidative haemolysis: Relationship to in vivo red cell survival. Br.J.Haematol. 27:587-595, 1974. * Steinberg, M.H. and Dreiling, B.J. Glucose-6-phosphate dehydrogenase deficiency in sickle cell anemia. Ann.Intern.Med. 80:217-220, 1974. * Szathmary, E.J.E., Cox, D.W., Gershowitz, H., Rucknagel, D.L., and Schanfield, M.S. The Northern and Southeastern Ojibwa:

Serum proteins and red cell enzyme systems. Am.J.Phys.Anthropol. 40:49-66, 1974. * Thigpen, J.T., Steinberg, M.H., Beutler, E., Gillespie, G.T.J., Dreiling, B.J., and Morrison, F.S. Glucose-6-phosphate dehydrogenase Jackson. A new variant associated with hemolytic anemia. Acta Haematol.(Basel) 51:310-314, 1974. Notes: (B396). * Turner, B.M., Fisher, R.A., and Harris, H. The age related loss of activity of four enzymes in the human erythrocyte. Clin.Chim.Acta 50:85-95, 1974. * Uddin, D.E., Dickson, L.G., and Brodine, C.E. Glucose-6-phosphate dehydrogenase deficiency in military recruits. JAMA 227:1408-1409, 1974. * Vergnes, H., Yoshida, A., Gourdin, D., Gherardi, M., Bierme, R., and Ruffie, J. Glucose-6-phosphate dehydrogenase Toulouse. A new variant with marked instability and severe deficiency discovered in a family of Mediterranean ancestry. Acta Haematol.(Basel) 51:240-249, 1974. * Waller, H.D., Birke, G., Tigges, F.-.J., and Benhr, H.C. Glutathiongehalt und Glutathion reduzierende Enzyme in Erythrocyten verschiedenen Alters. Klin.Wochenschr. 52:179-184, 1974. * Walls, R. and Hochstein, P. Glucose-6-phosphate dehydrogenase deficiency: A novel role for thyroxine in peroxide-induced hemolysis. Life Sci. 15:1757-1763, 1974. * Wang, Y.M., King, S.M., and Van Eys, J. Isocitrate metabolism in normal and glucose-6-phosphate dehydrogenase deficient red cells. Biochem.Med. 11:327-337, 1974. * Zatz, M., Itskan, S.B., Sanger, R., Frota-Pressoa, O., and Saldanha, P.H. New linkage data for the X-linked types of muscular dystrophy and G6PD variants, colour blindness, and Xg blood groups. J.Med.Genet. 11:321-327, 1974. * Bailey-Wood, R., Blayney, L.M., Muir, J.R., and Jacobs, A. The effects of iron deficiency on rat liver enzymes. Br.J.Exp.Pathol. 56:193-198, 1975. * Bansard-Desmidt, N. Essai de caracterisation de deux variantes erythrocytaires de la glucose-6- phosphate deshydrogenase chez un sujet presentant un deficit enzymatique partiel. Biomedicine 22:411-415, 1975. * Beutler, E. Diagnosis of G-6-PD deficiency. Lancet 2:1032-1033, 1975. Notes: (B434). * Beutler, E. and Matsumoto, F. Unpublished , 1975. * Bienzle, U., Sodeinde, O., Effiong, C.E., and Luzzatto, L. Glucose 6-phosphate dehydrogenase deficiency and sickle cell anemia: Frequency and features of the association in an African community. Blood 46:591-597, 1975. * Blume, K.G., Schmidt, G.M., Heissmeier, H.H., and Lhr, G.W. Hexose-6-phosphate dehydrogenase from human tissues: An electrophoretic study in health and disease. Experientia 31:496-497, 1975. * Buckley, R.D., Hackney, J.D., Clark, K., and Posin, C. Ozone and human blood. Arch.Environ.Health 30:40-43, 1975. * Campbell, G.D.,Jr., Steinberg, M.H., and Bower, J.D. Ascorbic acid-induced hemolysis in G-6-PD deficiency. Ann.Intern.Med. 82:810, 1975. * Carrell, R.W., Winterbourn, C.C., and Rachmilewitz, E.A. Activated oxygen and haemolysis. Br.J.Haematol. 30:259-264, 1975. * Catalano, E.W., Johnson, G.F., and Solomon, H.M. Measurement of erythrocyte glucose-6-phosphate dehydrogenase activity with

a centrifugal analyzer. Clin.Chem. 21:134-138, 1975. * Cayanis, E., Gomperts, E.D., Balinsky, D., Disler, P., and Myers, A. G6PD Hillbrow: A new variant of glucose-6-phosphate dehydrogenase associated with drug-induced haemolytic anaemia. Br.J.Haematol. 30:343-350, 1975. * Cederbaum, A.I. and Beutler, E. Nonspherocytic hemolytic anemia due to G-6-PD Grand Prairie. IRCS 3:579, 1975. Notes: (B428). * De Flora, A., Morelli, A., Benatti, U., and Giuliano, F. An improved procedure for rapid isolation of glucose 6-phosphate dehydrogenase from human erythrocytes. Arch.Biochem.Biophys. 169:362-363, 1975. * De Flora, A., Morelli, A., Giuliano, F., Benatti, U., and Radin, L. Human erythrocyte glucose 6-phosphate dehydrogenase. Influence of coenzyme derivatives on thermostability and kinetic properties. Ital.J.Biochem. 24:147-161, 1975. * Djerassi, L.S. and Vitany, L. Haemolytic episode in g6 pd deficient workers exposed to tnt. Br.J.Ind.Med. 32:54-58, 1975. * Endou, H. and Neuhoff, V. Kinetic studies of microsomal glucose dehydrogenase in rat liver. Hoppe-Seyler's Z.Physiol.Chem. 356:1381-1396, 1975. * Erickson, R. Mouse spermatozoal glucose-6-phosphate dehydrogenase is the x-linked form. Biochem.Biophys.Res.Commun. 63:1000-1004, 1975. * Gahr, M. and Schrter, W. Inhibition of normal red cell glucose 6-phosphate dehydrogenase (G-6-PD) by a variant enzyme, G-6-PD Hamburg. FEBS Lett. 59:237-240, 1975. * Ganesan, J., Eng, L.-.I., and Poon, O.B. Abnormal hemoglobins, glucose-6-phosphate dehydrogenase deficiency and hereditary ovalocytosis in the Dayaks of Sarawak. Hum.Hered. 25:258-262, 1975. * Glader, B. Role of elevated glucose concentrations in the hemolysis of glucose-6- phosphate dehydrogenase deficient erythrocytes. Proc.Soc.Exp.Biol.Med. 148:50-53, 1975. * Goebel, K.M., Goebel, F.D., Neitzert, A., Hausmann, L., and Schneider, J. Adaptation of red cell enzymes and intermediates in metabolic disorders. Enzyme 19:201-211, 1975. * Goldstein, S. and Moerman, E. Heat-labile enzymes in skin fibroblasts from subjects with progeria. N.Engl.J.Med. 292:1305-1309, 1975. * Gonzalez, R., Estrada, M., and Colombo, B. G-6-PD polymorphism and racial admixture in the Cuban population. Humangenetik 26:75-78, 1975. Notes: 3 of 303 "White" males had G6PD A. * Harley, J.D., Agar, N.S., and Gruca, M.A. Cataracts with a glucose-6-phosphate dehydrogenase variant. BMJ 2:86, 1975. * Herman, J. and Ben-Meir, S. Overt hemolysis in patients with glucose-6-phosphate dehydrogenase deficiency. Isr.J.Med.Sci. 2:340-344, 1975. * Hori, S.H., Yonezawa, S., Mochizuki, Y., Sado, Y., and Kamada, T. Evolutionary aspects of animal glucose 6-phosphate dehydrogenase isoyzmes. In: Isozymes IV. Genetics and Evolution. edited by Markert, C.L.New York:Academic Press, Inc. 1975,p. 839-852. * Julian, G.R. and Reithel, F.J. Glucose-6-phosphate dehydrogenase from bovine mammary gland. Methods Enzymol. 41:183-188, 1975. * Kahn, A., Bernard, J.-F., Cottreau, D., Marie, J., and Boivin, P. Gd(-)Abrami. A deficient G-6PD variant with hemizygous expression in blood cells of a woman with primary myelofibrosis.

Humangenetik 30:41-46, 1975. * Kahn, A., North, M.L., Messer, J., and Boivin, P. G-6-PD "Ankara". A new G-6PD variant with deficiency found in a Turkish family. Humangenetik 27:247-250, 1975. * Kahn, A., Hakim, J., Cottreau, D., and Boivin, P. Gd (-) Matam, an African glucose-6-phosphate dehydrogenase variant with enzyme deficiency. Biochemical and immunological properties in various hemopoietic tissues. Clin.Chim.Acta 59:183-190, 1975. * Kahn, A., Cottreau, D., Bernard, J.F., and Boivin, P. Post translational modifications of glucose-6-phosphate dehydrogenase in human leukemias. Biomedicine 22:539-594, 1975. * Khalil, M., Aziz, Y., Tanious, A., Mahmoud, S., and Gharib, B. Study of red cell membrane lipids in glucose-6-phosphate dehydrogenase deficiency anemia. Gazette of the Egyptian Paediatric Association 23:281-289, 1975. * Kirkman, H.N. and Gaetani, G.D. Glucose-6-phosphate deficiency and inhibition by NADPH: A self-contradictory argument. Science 190:171-172, 1975. * Kirkman, H.N., Gaetani, G.D., Clemons, E.H., and Mareni, C. Red cell NADP+ and NADPH in glucose-6-phosphate dehydrogenase deficiency. J.Clin.Invest. 55:875-878, 1975. * Kothe, K., Sachsenroeder, C.H., and Reich, J.G. Redox metabolism of glutathione in the red blood cell. Acta Biol.Med.Ger. 34:203-228, 1975. * Lampe, R.M., Kirdpon, S., Mansuwan, P., and Benenson, M.W. Glucose-6-phosphate dehydrogenase deficiency in Thai children with typhoid fever. J.Pediatr. 87:576-578, 1975. * Leipzig, R.M., Brewer, G.J., and Kruckeberg, W.C. Superoxide and G-6-PD-type hemolysis. Prog.Clin.Biol.Res. 1:711-726, 1975. * Linder, D., Kaiser McCaw, B., and Hecht, F. Parthenogenic origin of benign ovarian teratomas. N.Engl.J.Med. 292:63-66, 1975. * Malaka-Zafiriu, K., Tsiures, J., and Cassimos, C. D-glucaric acid excretion in newborns with severe jaundice of unknown etiology and due to glucose-6-phosphate dehydrogenase deficiency in Greece. Helv.Paediatr.Acta 30:201-207, 1975. * Mann, J.R., Cotter, K.P., Walker, R.A., Bird, G.W., and Stuart, J. Anaemic crisis in sickle cell disease. J.Clin.Pathol. 28:341-344, 1975. * McCurdy, P.R. and Morse, E.E. Glucose-6-phosphate dehydrogenase deficiency and blood transfusion. Vox Sang. 28:230-237, 1975. * Meloni, T., Costa, S., and Cutillo, S. Haptoglobin, hemopexin, hemoglobin and hematocrit in newborns with erythrocyte glucose-6-phosphate dehydrogenase deficiency. Acta Haematol.(Basel) 54:284-288, 1975. * Migeon, B.R. and Kennedy, J.F. Evidence for the inactivation of an X chromosome early in the development of the human female. Am.J.Hum.Genet. 27:233-239, 1975. * Mills, G.C., Alperin, J.B., and Trimmer, K.B. Studies on variant glucose-6-phosphate dehydrogenases: G6PD Fort Worth. Biochem.Med. 13:264-275, 1975. * North, M.L., Kahn, A., Messer, J., Willard, D., and Boivin, P. Ictere neo-natal et deficit en G-6-PD Ankara, une nouvelle variante enzymatique decouverte dans une famille Turque. Nouv.Rev.Fr.Hematol. 15:454-459, 1975. * Papiha, S.S., Roberts, D.F., Ali, S.G.M., and Islam, M.M. Some hereditary blood factors of the Bengali muslim of Bangladesh (red cell enzymes, haemoglobins, and serum proteins). Humangenetik 28:285-293, 1975.

* Pawlak, A.L., Mazurkiewicz, C.A., Ordynski, J., Rozynkowa, D., and Horst, A. G-6-PD Poznan, variant with severe enzyme deficiency. Humangenetik 28:163-165, 1975. * Pearson, T.A., Wang, A., Solez, K., and Heptinstall, R.H. Clonal characteristics of fibrous plaques and fatty streaks from human aortas. Am.J.Pathol. 81:379-387, 1975. * Race, R.R. and Sanger, R. XG and X-chromosome mapping. In: Blood Groups in Man,Anonymous London:Blackwell Scientific, 1975,p. 594-618. * Sansone, G., Perroni, L., and Yoshida, A. Glucose-6-phosphate dehydrogenase variants from Italian subjects associated with severe neonatal jaundice. Br.J.Haematol. 31:159-165, 1975. * Shatskaya, T.L., Krasnopolskaya, K.D., and Annenkov, G.A. A description of new mutant forms of erythrocyte glucose-6-phosphate dehydrogenase isolated at the territory of the Soviet Union. Genetika 11:116-122, 1975. * Van Der Staak, W.B.J. and Cotton, D.W.K. D-penicillamine and haemolytic anaemia. Lancet 1:1430, 1975. * Vergnes, H., Gherardi, M., and Bouloux, C. Erythrocyte glucose-6-phosphate dehydrogenase in the Niokolonko (Malinke of the Niokolo) of Eastern Senegal. Identification of a slow variant with normal activity (Tacoma-like). Hum.Hered. 25:80-87, 1975. * Vuopio, P., Harkonen, M., Helske, T., and Naeveri, H. Red cell glucose-6-phosphate dehydrogenase deficiency in finland. Characterization of a new variant with severe enzyme deficiency. Scand.J.Haematol. 15:145-152, 1975. * Weaver, D.D., Gartler, S.M., Boue, A., and Boue, J. Evidence for two active X chromosomes in a human XXY triploid. Humangenetik 28:39-42, 1975. * Wood, T.A., Tooze, J.A., and Dunbar, E. Diagnosis of g.-6-P.D. Deficiency. Lancet 2:657-Letter, 1975. * Woodfield, D.G. and Biddulph, J. Neonatal jaundice and glucose-6-phosphate dehydrogenase deficiency in Papua New Guinea. Med.J.Aust. 1:443-446, 1975. * Worathumrong, N. and Grimes, A.J. The effect of o-salicylate upon pentose phosphate pathway activity in normal and G6PD-deficient red cells. Br.J.Haematol. 30:225-231, 1975. * Yoshida, A., Baur, E., and Voigtlander, B. Unpublished , 1975. Notes: G6PD Steilacoomb, Tacoma, Western. * Yoshida, A. Purification of human red cell glucose 6-phosphate dehydrogenase by affinity chromatography. J.Chromatogr. 114:321-327, 1975. * Yoshida, A. Glucose-6-phosphate deficiency and inhibition by NADPH:A self-contradictory argument (reply). Science 190:172, 1975. * Yoshida, A. Evolution of glucose 6-phosphate dehydrogenase and hexose 6-phosphate dehydrogenase. In: Isozymes IV. Genetics and Evolution. edited by Markert, C.L.New York:Academic Press, Inc. 1975,p. 853-866. * Abeyaratne, K.P., Premawansa, S., Rajapakse, L., Roberts, D.F., and Papiha, S.S. A survey of glucose-6-phosphate-dehydrogenase deficiency in the North central province of Sri Lanka (formerly Ceylon). Am.J.Phys.Anthropol. 44:135-138, 1976. * Adamson, J.W., Fialkow, P.J., Murphy, S., Prchal, J.F., and Steinmann, L. Polycythemia vera: Stem-cell and probable clonal origin of the disease. N.Engl.J.Med. 295:913-916, 1976. * Babalola, A.O.G., Beetlestone, J.G., and Luzzatto, L.

Genetic variants of human erythrocyte glucose-6-phosphate dehydrogenase. J.Biol.Chem. 251:2993-3002, 1976. * Baylin, S.B., Ganns, D.S., and Hsu, S.H. Clonal origin of inherited medullary thyroid carcinoma and pheochromocytoma. Science 193:321-323, 1976. * Bensinger, T.A. and Medina, F. Excessive pyruvate accumulation in G-6-PD deficient (G-6-PD-def) erythrocytes during liquid storage. Blood 48:993, 1976. * Bensinger, T.A. Prolonged maintenance of 2,3 diphosphoglycerate (2,3-DPG) in glucose-6-P dehydrogenase (G6PD) deficient stored blood. Clin.Res. 24:107A, 1976. * Berger, H. Enzyme-diseases in childhood. Wien.Med.Wochenschr. 126:501-504, 1976. * Beutler, E., Keller, J.W., and Matsumoto, F. A new glucose-6-P dehydrogenase (G-6-PD) variant associated with nonspherocytic hemolytic anemia: G-6-PD Atlanta. IRCS 4:579, 1976. Notes: (B451). * Beutler, E. Glucose-6-phosphate dehydrogenase deficiency: A new Indian variant, G-6-PD Jammu. In: Trends in Haematology, edited by Sen, N.N. and Basu, A.K.Calcutta:K.P. Bagchi & Co. 1976,p. 279-283. Notes: (B441). * Beutler, E., Matsumoto, F., Warner, J., Powars, D., and Kan, Y.W. Glutathione peroxidase (GSH Px) activity in alpha-thalassemia and in G-6-PD deficiency. Blood 48:967, 1976. Notes: (B453). * Bhasin, M.K., Singh, I.P., and Singh, K. Glucose-6-phosphate dehydrogenase. I. Variants - a review. Ind.J.Phys.Anthropol.Hum.Genet 2:79-111, 1976. * Bienzle, U., Effiong, C., and Luzzatto, L. Erythrocyte glucose 6-phosphate dehydrogenase deficiency (G6PD type A-) and neonatal jaundice. Acta Paediatr.Scand. 65:701-703, 1976. * Bienzle, U., Effiong, C.E., Aimaku, V.E., and Luzzatto, L. Erythrocyte enzymes in neonatal jaundice. Acta Haematol.(Basel) 55:10-20, 1976. * Brewer, G.J. and Zarafonetis, J.D. The haemolytic effect of various regimens of primaquine with chloroquine in American negroes with G6PD deficiency and the lack of an effect of various antimalarial suppressive agents on erythrocyte metabolism. Bull.WHO 36:303-308, 1976. * Carandina, G., Moretto, E., Zecchi, G., and Conighi, C. Glucose-6-phosphate dehydrogenase Ferrara. A new variant of G-6-PD identified in Northern Italy. Acta Haematol.(Basel) 56:116-122, 1976. * Carpentieri, U., Moore, R.L., and Nichols, M.M. Kernicterus in a newborn female with G-6-PD deficiency. J.Pediatr. 89:854-855, 1976. * Cederbaum, S.D. and Yoshida, A. Glucose 6-phosphate dehydroenase in rainbow trout. Biochem.Genet. 14:245-258, 1976. * Chan, T.K., Todd, D., and Tso, S.C. Drug-induced haemolysis in glucose-6-phosphate dehydrogenase deficiency. BMJ 2:1227-1229, 1976. * Chapman, V.M. and Shows, T.B. Somatic cell genetic evidence for X-chromosome linkage of three enzymes in the mouse. Nature 259:665-667, 1976. * Cottreau, D., Kahn, A., and Boivin, P. Human platelet glucose-6-phosphate dehydrogenase. Total purification, kinetic studies and relationship with enzyme from other blood cells. Enzyme 21:142-151, 1976.

* Crowley, C. and Necheles, T.F. Hereditary disorders of the erythrocyte. Clin.Perinatol. 3:161-175, 1976. * Esters, A. and Habedank, M. Glucose-6-phosphatdehydrogenase-mangel in drei generationen einer aachener familie. Mschr.Kinderheik. 124:314-316, 1976. * Fialkow, P.J. Clonal origin of human tumors. Biochim.Biophys.Acta 458:283-321, 1976. * Friedman, J.M. and Fialkow, P.J. Viral "tumorigenesis" in man: Cell markers in condylomata acuminata. Int.J.Cancer 17:57-61, 1976. * Gaetani, G.D., Mareni, C., Ravazzolo, R., and Salvidio, E. Haemolytic effect of two sulphonamides evaluated by a new method. Br.J.Haematol. 32:183-191, 1976. * Gahr, M., Bornhalm, D., and Schrter, W. Haemolytic anaemia due to glucose-6-phosphate dehydrogenase (G6PD) deficiency: Demonstration of two new biochemical variants, G6PD Hamm and G6PD Tarsus. Br.J.Haematol. 33:363-370, 1976. * Gahr, M., Schrter, W., Sturzenegger, M., Bornhalm, D., and Marti, H.R. Glucose-6-phosphate dehydrogenase (G-6-PD) deficiency in Switzerland. Helv.Paediatr.Acta 31:159-166, 1976. * Ganzoni, A.M., Barras, J.P., and Marti, H.R. Red cell ageing and death. Vox Sang. 30:161-174, 1976. * Gherardi, M., Bierme, R., Corberand, J., Pris, J., and Vergnes, H. Distribution of G6PD types in the population of Southwest France: Common variants and new variants. Hum.Hered. 26:279-289, 1976. * Glader, B. Evaluation of the hemolytic role of aspirin in glucose-6-phosphate dehydrogenase deficiency. J.Pediatr. 89:1027-1028, 1976. * Gonzalez, R., Ballester, J.M., Estrada, M., Lima, F., Martinez, G., Wade, M., Colombo, B., and Vento, R. A study of the genetical structure of the Cuban population: Red cell and serum biochemical markers. Am.J.Hum.Genet. 28:585-596, 1976. Notes: Among 155 "white" Cubans the incidence of G6PD A was .0325. * Grunwald, M. and Hill, H.Z. Characterization of the glucose 6-phosphate dehydrogenase activity in rat liver mitochondria. Biochem.J. 159:683-687, 1976. * Guidi, G., Solero, P., and Schiavon, R. Deficit eritrocitario di glucosio-6-fosfato deidrogenasi: Un semplice e rapido procedimento di screening. Lab 3:495-498, 1976. * Gulati, P.D. and Rizvi, S.N.A. Acute reversible renal failure in G-6 PD-deficient siblings. Postgrad.Med.J. 52:83-85, 1976. * Jacobson, R.J. and Fialkow, P.J. Idiopathic myelofibrosis: Stem cell abnormality and probable neoplastic origin. Clin.Res. 24:439A, 1976. * Kahn, A., Boivin, P., Rubinson, H., Cottreau, D., Marie, J., and Dreyfus, J.-C. Modifications of purified glucose-6-phosphate dehydrogenase and other enzymes by a factor of low molecular weight abundant in some leukemic cells. Proc.Natl.Acad.Sci.USA 73:77-81, 1976. * Kahn, A., Esters, A., and Habedank, M. Gd(-)Aachen, a new variant of deficient glucose-6-phosphate dehydrogenase. Hum.Genet. 32:171-180, 1976. * Kahn, A., Bertrand, O., Cottreau, D., Boivin, P., and Dreyfus, J. Studies on the nature of different molecular forms of glucose-6-phosphate dehydrogenase purified from human leukocytes. Biochim.Biophys.Acta 445:537-548, 1976. * Kanji, M.I., Toews, M.L., and Carper, W.R.

Glucose-6-phosphate dehydrogenase. Purification and partial characterization. J.Biol.Chem. 251:2255-2257, 1976. * Kanji, M.I., Toews, M.L., and Carper, W.R. A kinetic study of glucose-6-phosphate dehydrogenase. J.Biol.Chem. 251:2258-2262, 1976. * Kleihauer, E. and Kohne, E. Toxische hemolytische anemien. Blut 33:73-82, 1976. * Lapierre, J., Holler, C., Tourte-Schaefer, C., Lebas-Saison, E., Launois, J.P., and Cachin, M. Haemolytic anaemia following anti-bilharzia treatment using niridazole in a woman of caribbean origin with g pd deficiency. Nouv.Presse Med. 5:147, 1976. * Lavelle, K.J., Atkinson, K.F., and Kleit, S.A. Case report: Hyperlactatemia and hemolysis in G6PD deficiency after nitrofurantoin ingestion. Am.J.Med.Sci. 272:201-204, 1976. * Lisker, R., Pere-Brice, N.O.R., Sosa, R., and Shein, M. Aspectos hereditarios y epidemiologicos de la deficiencia de glucosa-6- deshidrogenasa erithrocitica en Mexico. Gac.Med.Mex. 111:454-458, 1976. * Mareni, C. and Gaetani, G.F.D. NADP+ and NADPH in glucose-6-phosphate dehydrogenase-deficient erythrocytes under oxidative stimulation. Biochim.Biophys.Acta 430:395-398, 1976. * Miwa, S., Ono, J., Nakashima, K., Abe, S., Kageoka, T., Shinohara, K., Isobe, J., and Yamaguchi, H. Two new glucose 6-phosphate dehydrogenase variants associated with congenital nonspherocytic hemolytic anemia found in Japan: Gd(-) Tokushima and Gd(-) Tokyo. Am.J.Hematol. 1:433-442, 1976. * Miwa, S. Congenital hemolytic anemias: A review of recent progress. Bull.Yamaguchi Med.School 23:131-163, 1976. * Morelli, A., Benatti, U., Guiliano, F., and De Flora, A. Human erythrocyte glucose-6-phosphate dehydrogenase. Evidence for competitive binding of NADP and NADPH. Biochem.Biophys.Res.Commun. 70:600-606, 1976. * Orzalesi, N., Sorcinelli, R., and Binaghi, F. Glucose-6-phosphate dehydrogenase in cataracts of subjects suffering from favism. Ophthalmic Res. 8:192-194, 1976. * Perkins, R.P. The significance of glucose-6-phosphate dehydrogenase deficiency in pregnancy. Am.J.Obstet.Gynecol. 125:215-223, 1976. * Piller, G., Rainer, H., Maurer, L., and Moser, K. Saeulenchromatographische Anreicherung der "Glukose-6-phosphatdehydrogenase Wien". Wien.Klin.Wochenschr. 88:6-9, 1976. * Rappelli, A., Glorioso, N., Tedde, R., Madeddu, P., and Campus, S. Impaired renin release after repetitive upright stimulation in G-6-PD deficiency subjects. IRCS 4:423, 1976. * Rinaldi, A., Filippi, G., and Siniscalco, M. Variability of red cell phenotypes between and within individuals in an unbiased sample of 77 heterozygotes for G6PD deficiency in Sardinia. Am.J.Hum.Genet. 28:496-505, 1976. * Romeo, G., Rinaldi, A., Urbano, F., and Filippi, G. Hair root versus red cell individual phenotype in Sardinian heterozygotes for G6PD deficiency (Mediterranean type). Am.J.Hum.Genet. 28:506-513, 1976. * Saha, N., Kirk, R.L., Shanbhag, S., Joshi, S.R., and Bhatia, H.M. Population genetic studies in kerala and the nilgiris (South West India). Hum.Hered. 26:175-197, 1976. * Schiliro, G., Russo, A., Mauro, L., Pizzarelli, G., and Marino, S. Leukocyte function and characterization of leukocyte glucose-6-phosphate dehydrogenase in Sicilian mutants. Pediatr.Res. 10:739-742, 1976.

* Schoos-Barbette, S., Dodinval-Versie, J., and Lambotte, C. Modification of neonatal screening test for erythrocyte glucose-6-phosphate dehydrogenase deficiency. Clin.Chim.Acta 71:239-244, 1976. * Shatskaya, T.L., Krasnopolskaya, K.D., and Idelson, L.I. The new form of glucose-6-phosphate dehydrogenase (G6PD "Kaluga") from erythrocytes of a patient with chronic non-spherocytic hemolytic anemia. Vopr.Med.Khim. 22:764-768, 1976. * Shatskaya, T.L., Krasnopolskaya, K.D., and Idelson, L.J. Mutant forms of erythrocyte glucose-6-phosphate dehydrogenase in Ashkenazi. Description of two new variants: G6PD Kirovograd and G6PD Zhitomir. Hum.Genet. 33:175-178, 1976. * Smith, J.E., Ryer, K., and Wallace, L. Glucose-6-phosphate dehydrogenase deficiency in a dog. Enzyme 21:379-382, 1976. * Smith, M.B. The incidence of glucose-6-phosphate dehydrogenase deficiency in a population of Greek, Italian and Yugoslav origin in Australia. Med.J.Aust. 2:485-486, 1976. * Swaminathan, R., Segall, N.H., Chapman, C., and Morgan, D.B. Red-blood-cell composition in thyroid disease. Lancet 2:1382-1385, 1976. * Tan, S.G. and Ashton, G.C. An autosomal glucose-6-phosphate dehydrogenase (hexose-6-phos-phate dehydrogenase) polymorphism in human saliva. Hum.Hered. 26:113-123, 1976. * Thomas, M., Agnus, D., Poirot, J.-.L., and Golvan, Y.-.J. Hemolysis induced by niridazole in two patients with deficiency of G-6-PD. Nouv.Presse Med. 5:1537-1538, 1976. * Vergnes, H., Gherardi, M., and Yoshida, A. G6PD Lozere and Trinacria-like. Segregation of two non hemolytic variants in a French family. Hum.Genet. 34:293-298, 1976. * Walls, R., Sree-Kumar, K., and Hochstein, P. Aging of human erythrocytes. Differential sensitivity of young and old erythrocytes to hemolysis induced by peroxide in the presence of thyroxine. Arch.Biochem.Biophys. 174:463-468, 1976. * Wild, D. and Hellkuhl, B. Isolation of mammalian cell mutants deficient in glucose 6-phosphate dehydrogenase by means of a replica-plating technique. Hum.Genet. 32:315-322, 1976. * Williams, A.O., Tugwell, P., and Edington, G.M. Glucose-6-phosphate dehydrogenase deficiency and lobar pneumonia. Arch.Pathol.Lab.Med. 100:25-31, 1976. * Wilson, W.W. Congenital hemolytic anemia due to deficiency of glucose-6-phosphate dehydrogenase. Rocky Mt.Med.J. 73:160-162, 1976. * Zaidman, J.L., Leiba, H., Scharf, S., and Steinman, I. Red cell glucose-6-phosphate dehydrogenase deficiency in ethnic groups in Israel. Clin.Genet. 9:131-133, 1976. * Anonymous Monoclonal theory of atheroma. BMJ 1:1371-1372, 1977. * Batischev, A.I. and Chernyak, N.B. A new anomalous variant of glucose-6-phosphoric dehydrogenase "Kremenchung" connected with acute drug hemolytic anemia. Probl.Gematol.Pereliv.Krovi. 22:47, 1977. * Batischev, A.I., Chernyak, N.B., and Torakev, Y.N. Detection of a new abnormal variant of glucose-6-phosphate dehydrogenase in human red cells. Bull.Eksperimental' Noi.Bi. 84:728-731, 1977. * Battistuzzi, G., Esan, G.J.F., Fusuan, F.A., Modiano, G., and Luzzatto, L. Response to Nance letter. Am.J.Hum.Genet. 29:543-544, 1977. * Battistuzzi, G., Esan, G.J.F., Fasuan, F.A., Modiano, G., and Luzzatto, L. Comparison of GdA and GdB activities in

Nigerians. A study of the variation of the G6PD activity. Am.J.Hum.Genet. 29:31-36, 1977. * Berry, E. and Melmed, R.N. Infectious hepatitis and glucose-6-phosphate dehydrogenase deficiency. Isr.J.Med.Sci. 13:600-603, 1977. * Beutler, E. Glucose 6-phosphate dehydrogenase deficiency. In: Hematology, edited by Williams, W.J., Beutler, E., Erslev, A.J., and Rundles, R.W.New York:McGraw-Hill, Inc. 1977,p. 466-479. Notes: (B487). * Beutler, E. Glucose-6-phosphate dehydrogenase deficiency and red cell glutathione peroxidase. Blood 49:467-469, 1977. Notes: (B462). * Beutler, E. and Matsumoto, F. A new glucose-6-phosphate dehydrogenase variant: G-6-PD (-) Los Angeles. IRCS 5:89, 1977. Notes: (B457). * Calabrese, E.J., Kojola, W.H., and Carnow, B.W. Ozone: A possible cause of hemolytic anemia in glucose-6-phosphate dehydrogenase deficient individuals. J.Toxicol.Environ.Health 2:709-712, 1977. * Cayanis, E., Lane, A.B., Jenkins, T., Nurse, G.T., and Balinsky, D. Glucose-6-phosphate dehydrogenase Porbandar: A new slow variant with slightly reduced activity in a South African family of Indian descent. Biochem.Genet. 15:765-773, 1977. * Chen, S., Anderson, J.E., Giblett, E.R., and Stamatoyannopoulos, G. Isozyme patterns in erythrocytes from human fetuses. Am.J.Hematol. 3:23-28, 1977. Notes: Starch gel electrophoretic patterns of 26 enzymes (corresponding to 36 gene loci) were examined in hemolysates of erythrocytes from 11 first-trimester and mid-trimester human fetuses (65-138 gestation days). The zymograms of 16 enzymes were identical in fetal and control adult red cells. Six enzymes (enolase, guanylate kinase, lactate dehydrogenase, nucleoside phosphorylase, phosphofructokinase, hexokinase) showed differences in the staining intensity of certain isozyme zones as compared with the controls. Also, the fetal red cell zymograms, in contrast to those of adults, contained the mitochondrial forms of isocitric dehydrogenase and glutamic oxaloacetic transaminase as well as more definite zones of phosphoglucomutase-3. Finally, some of the isozymes of uridine diphosphate kinase in the fetal cells had slightly retarded mobility. These observed differences between fetal and adult red cells could reflect the expression of a different program of protein synthesis in red cells of the fetuses or * Chernyak, N.B., Batischev, A.I., and Tokarev, Y.N. Characteristics of a new abnormal variant of G-6-PD in human red cells. Acta Biol.Med.Ger. 36:753-758, 1977. * Chernyak, N.B., Batischev, A.I., Lamzina, N.V., Tokarev, Y.N., and Alexeev, G.A. Electrophoretic and kinetic properties of glucose-6-phosphate dehydrogenase from erythrocytes or patients with hemolytic anemia, related to deficiency of the enzyme activity. Vopr.Med.Khim. 23:166-171, 1977. * Dash, S. and Bhagwat, A.G. Combined G-6PD and 6-PGD deficiency in a Hindu boy. Acta Haematol.(Basel) 57:351-353, 1977. * Drew, J.H., Smith, M.B., and Kitchen, W.H. Glucose-6-phosphate dehydrogenase deficiency in immigrant Greek infants. J.Pediatr. 90:659-660, 1977. * Feldman, R., Gromisch, D.S., Luhby, A.L., and Beutler, E. Congenital nonspherocytic hemolytic anemia due to

glucose-6-phosphate dehydrogenase East Harlem: A new deficient variant. J.Pediatr. 90:89-91, 1977. Notes: (B460). * Fried, D., Gotlieb, A., and Roitman, A. Infectious hepatitis with excessive hyperbilirubinemia and a hemolytic crisis in an 8-year-old boy. Clin.Pediatr. 16:482-483, 1977. * Gelpi, A.P. and King, M.C. New data on glucose-6-phosphate dehydrogenase deficiency in Saudi Arabia. Hum.Hered. 27:285-291, 1977. * Gonzalez, R., Wade, M., Estrada, M., Svarch, E., and Colombo, B. G6PD Pinar del Rio: A new variant discovered in a Cuban family. Biochem.Genet. 15:909-913, 1977. * Heinitz, M. Significance of diminished erythrocyte 6 phosphate dehydrogenase activity in chronic schizophrenia. Therapiewoche 27:1732-1736, 1977. * Hutz, M.H., Yoshida, A., and Salzano, F.M. Three rare G-6-PD variants from Porto Alegre, Brazil. Hum.Genet. 39:191-197, 1977. * Javadov, R.B., Grinberg, L.N., Krasnova, S.N., Makhmudova, S.A., and Troitskaya, O.V. Hemoglobinopathies and glucose-6-phosphate dehydrogenase deficiency in one of the regions of Azerbaijan: Mass screening and laboratory investigations. Acta Biol.Med.Ger. 36:709-715, 1977. * Johnson, G.J., Kaplan, M.E., and Beutler, E. G-6-PD Long Prairie: A new mutant exhibiting sensitivity to inhibition by NADPH and accompanied by nonspherocytic hemolytic anemia. Blood 49:247-251, 1977. Notes: (B459). * Kahn, A., Bertrand, O., Cottreau, D., Boivin, P., and Dreyfus, J.-C. Evidence for structural differences between human glucose-6-phosphate dehydrogenase purified from leukocytes and erythrocytes. Biochem.Biophys.Res.Commun. 77:65-72, 1977. * Kahn, A., Guillouzo, A., Cottreau, D., Marie, J., Bourel, M., Boivin, P., and Dreyfus, J.-C. Accuracy of protein synthesis and in vitro aging. Gerontology 23:174-184, 1977. * Kahn, A., Boyer, C., Cottreau, D., Marie, J., and Boivin, P. Immunologic study of the age-related loss of activity of six enzymes in the red cells from newborn infants and adults -evidence for a fetal type of erythrocyte phosphofructokinase. Pediatr..Res. 11:271-276, 1977. * Kahn, A., Dao, C., Cottreau, D., and Bilski-Pasquier, G. 'GD (-) Hotel Dieu': A new G-6PD variant with chronic hemolysis in a negro patient from Senegal. Hum.Genet. 39:353-357, 1977. * Kahn, A., Guillouzo, A., Leibovitch, M.-.P., Cottreau, D., Bourel, M., and Dreyfus, J.-C. Heat lability of glucose-6-phosphate dehydrogenase in some senescent human cultured cells. Evidence for its postsynthetic nature. Biochem.Biophys.Res.Commun. 77:760-766, 1977. * Krasnopolskaya, K.D., Shatskaya, T.L., Filippov, I.K., Annenkov, G.A., Zakharova, T.V., Mekhtiev, N.K., and Movsum-Zade, K.M. Genetic heterogeneity of G 6 PD deficiency: Study of mutant alleles in Shekii district of Azerbaijan. Genetika 13:984-988, 1977. * Lisker, R., Briceno, R.P., Zavala, C., Navarrete, J.I., Wessels, M., and Yoshida, A. A glucose 6-phosphate dehydrogenase Gd (-) Castilla variant characterized by mild deficiency associated with drug induced hemolytic anemia. J.Lab.Clin.Med. 90:754-759, 1977. * Mandelli, F., Amadori, S., De Laurenzi, A., Kahn, A., Isacchi, G., and Papa, G. Glucose-6-phosphate dehydrogenase

Velletri. Acta Haematol.(Basel) 57:121-126, 1977. * Marti, H.R., Fischer, S., and Killer, D. Characterization of abnormal glucose-6-phosphate dehydrogenase variants. Acta Biol.Med.Ger. 36:703-708, 1977. * Miwa, S., Nakashima, K., Ono, J., Fujii, H., and Suzuki, E. Three glucose 6-phosphate dehydrogenase variants found in Japan. Hum.Genet. 36:327-334, 1977. Notes: G 6 PD Ogori, Hofu, & Mediterannean-like. * Nakashima, K. and Yoshida, A. Problems of indirect immunologic assay of specific enzyme activity. J.Lab.Clin.Med. 89:446-454, 1977. * Nakashima, K., Ono, J., Abe, S., Miwa, S., and Yoshida, A. G6PD Ube, a glucose-6-phosphate dehydrogenase variant found in four unrelated Japanese families. Am.J.Hum.Genet. 29:24-30, 1977. * Nance, W.E. Quantitative studies of glucose-6-phosphate dehydrogenase. Am.J.Hum.Genet. 29:537-542, 1977. * Pawlak, A.L. and Rozynkowa, D. Parallel occurrence of oxidant-sensitivity and decreased inhibition by NADPH in G-6-PD Poznan. Hum.Genet. 40:107-111, 1977. * Pearson, T.A., Kramer, E.C., Solez, K., and Heptinstall, R.H. The human atherosclerotic plaque. Am.J.Pathol. 86:657-664, 1977. * Roeckel, I.E. Transfusion requirements of patients with enzyme deficient red cells. Ann.Clin.Lab.Sci. 7:511-514, 1977. * Rubins, J. and Young, L.E. Hereditary spherocytosis and glucose-6-phosphate dehydrogenase deficiency. Double hemolytic jeopardy. JAMA 237:797-798, 1977. * Sansone, G., Perroni, L., Yoshida, A., and Dave, V. A new glucose-6-phosphate dehydrogenase variant (GD Trinacria) in two unrelated families of Sicilian ancestry. Ital.J.Biochem. 26:44-50, 1977. * Sarkar, S., Nelson, A.J., and Jones, O.W. Glucose-6-phosphate dehydrogenase (G6PD) activity of human sperm. J.Med.Genet. 14:250-255, 1977. * Singh, R.N., Gupta, B.D., Gupta, M., and Kochar, S. A comparative study of furazolidone and metronidazole in giardiasis. Indian J.Pediatr. 44:183-188, 1977. Notes: Jaundice only. * Swarup-Mitra, S. Activity of glutathione peroxidase and glutathione reductase in G-6-PD deficient subjects. Indian J.Med.Res. 66:253-259, 1977. * Tan, K.L. Phototherapy for neonatal jaundice in erythrocyte glucose-6-phosphate dehydrogenase-deficient infants. Pediatrics 59:1023-1026, 1977. * Tillmann, W., Gahr, M., Labitzke, N., and Schrter, W. Membrane deformability of erythrocytes with glucose-6-phosphate dehydrogenase hamburg. Acta Haematol.(Basel) 57:162-167, 1977. * Tillmann, W., Labitzke, N., and Schrter, W. Guenstige rheologische Eigenschaften der Erythrozyten beim Glucose-6phosphatdehydrogenase-mangel. Klin.Wochenschr. 55:385-391, 1977. * Udomratn, T., Steinberg, M.H., Campbell, G.D.J., and Oelshlegel, F.J.J. Effects of ascorbic acid on glucose-6-phosphate dehydrogenase-deficient erythrocytes: Studies in an animal model. Blood 49:471-475, 1977. * Usanga, E.A., Bienzle, U., Cancedda, R., Fasuan, F.A., Ajayi, O., and Luzzatto, L. Genetic variants of human erythrocyte glucose 6-phosphate dehydrogenase: New variants in West Africa characterized by column chromatography. Ann.Hum.Genet. 40:279-286, 1977. * Van Ros, G. La variante Africaine du deficit en

glucose-6-phosphate deshydrogenase comme facteur favorisant d'anemie: Enquete comparative portant sur 157 adultes defiients et 300 non-deficients. Ann.Soc.Belg.Med.Trop. 57:39-49, 1977. * Allen, D.W., Johnson, G.J., Cadman, S., and Kaplan, M.E. Membrane polypeptide aggregates in glucose-6-phosphate dehydrogenase deficient and in vitro aged red blood cells. J.Lab.Clin.Med. 91:321-327, 1978. * Benabadji, M., Merad, F., Benmoussa, M., Trabuchet, G., Junien, C., Dreyfus, J.C., and Kaplan, J.C. Heterogeneity of glucose-6-phosphate dehydrogenase deficiency in Algeria. Hum.Genet. 40:177-184, 1978. * Benatti, U., Morelli, A., Frascio, M., Melloni, E., Salamino, F., Sparatore, B., Pontremoli, S., and De Flora, A. Glucose 6-phosphate dehydrogenase activity in membranes of erythrocytes from normal individuals and subjects with Mediterranean G6PD deficiency. Biochem.Biophys.Res.Commun. 85:1318-1324, 1978. * Beutler, E. and Phyliky, R.L. Unpublished , 1978. Notes: G 6 PD Waterloo. Patient Maynard Ellison. * Beutler, E. Glucose 6 phosphate dehydrogenase deficiency. In: The Metabolic Basis of Inherited Disease, edited by Stanbury, J.B., Wyngaarden, J.B., and Fredrickson, D.S.New York:McGraw-Hill, Inc. 1978,p. 1430-1450. Notes: (B503). * Beutler, E. and West, C. Glucose-6-phosphate dehydrogenase variants in the chimpanzee. Biochem.Med. 20:364-370, 1978. Notes: (B534). * Corberand, J., De Larrard, B., Vergnes, H., and Carriere, J.P. Chronic granulomatous disease with leukocytic glucose-6-phosphate dehydrogenase deficiency in a 28-month-old girl. Am.J.Clin.Pathol. 70:296-300, 1978. * Deutsch, J. Maleimide as a inhibitor in measurement of erythrocyte glucose-6-phosphate dehydrogenase activity. Clin.Chem. 24:885-889, 1978. * Edgell, C.S., Kirkman, H.N., Clemons, E., and Buchanan, P.D. Prenatal diagnosis by linkage: Hemophilia A and polymorphic glucose-6-phosphate dehydrogenase. Am.J.Hum.Genet. 30:80-84, 1978. * Fialkow, P.J., Reddy, A.L., Najfeld, V., and Singer, J. Chronic lymphocytic leukemia: Clonal origin in a committed b-lymphocyte progenitor. Lancet 2:444-445, 1978. * Galliano, S., Mareni, C., and Gaetani, G.F.D. Effect of hemolysis on the hexose monophosphate pathway in normal and in glucose-6-phosphate dehydrogenase-deficient erythrocytes. Biochim.Biophys.Acta 501:1-9, 1978. * Gerli, G.C., Agostoni, A., and Fiorelli, G. G-6pd loading of g-6pd-deficient erythrocytes. Experientia 34:431-432, 1978. * Griffin, J.P., McLaren, G.D., and Muir, W.A. Evidence for the multicellular origin of primary thrombocytosis. Blood 52 (Supplement 1):162, 1978. * Houben, A. and Remacle, J. Lysosomal and mitochondrial heat labile enzymes in ageing human fibroblasts. Nature 275:59-60, 1978. * Janakiraman, N., Seeler, R.A., Royal, J.E., and Chen, M.F. Hemolysis during BAL chelation therapy for high blood lead levels in two G 6 PD deficient children. Clin.Pediatr. 17:485-487, 1978. * Kahn, A., Vibert, M., Cottreau, D., Skala, H., and Dreyfus, J.C. Hyperanodic forms of human glucose-6-phosphate dehydrogenase. Biochim.Biophys.Acta 526:318-327, 1978. * Kahn, A., North, M.L., Cottreau, D., Giron, G., and Lang,

J.M. G6PD Vientiane: A new glucose-6-phosphate dehydrogenase variant with increased stability. Hum.Genet. 43:85-89, 1978. * Kahn, A. G 6 PD variants. Hum.Genet. , 1978. * Kate, S.L., Mukherjee, B.N., Malhotra, K.C., Phadke, M.A., Mutalik, G.S., and Sainani, G.S. Red cell glucose-6-phosphate dehydrogenase deficiency and haemoglobin variants among ten endogamous groups of Maharashtra and West Bengal. Hum.Genet. 44:339-343, 1978. * Kwiatkowska, J., Kwiatkowska, D., Andrzejak, R., and Zatonski, W. Acquired enzymopathy of erythrocyte glucose-6-phosphate dehydrogenase in acute viral hepatitis. Clin.Chim.Acta 83:75-79, 1978. * Lexomboon, U. and Unkurapiana, N. Co-trimoxazole in the treatment of typhoid fever in children with glucose-6-phosphate dehydrogenase deficiency. Southeast Asian J.Trop.Med.Public Health 9:576-80, 1978. * Lisker, R., Briceno, R.P., Agrilar, L., and Yoshida, A. A variant glucose-6-phosphate dehydrogenase Gd (-) Chiapas. Associated with moderate enzyme deficiency and occasional hemolytic anemia. Hum.Genet. 43:81-84, 1978. * Luzzatto, L. and Testa, U. Human erythrocyte glucose-6-phosphate dehydrogenase: Structure and function in normal and mutant subjects. In: Current Topics in Hematology, edited by Piomelli, S. and Yachnin, S.New York:Alan R. Liss, Inc. 1978,p. 1-70. * Meloni, T., Costa, S., Corti, R., and Cutillo, S. Agar in control of hyperbilirubinemia of full-term newborn infants with erythrocyte G-6-PD deficiency. Biol.Neonate 34:295-298, 1978. * Meloni, T., Costa, S., Corti, R., and Cutillo, S. Salicylamide glucuronide formation in newborn babies with G 6 PD deficiency. Biol.Neonate 33:189-192, 1978. * Miwa, S., Fujii, H., Nakatsuji, T., Ishida, Y., Oda, E., Kaneto, A., Motokawa, M., Ariga, Y., Fukuchi, S., Sasai, S., Hiraoka, K., Kashii, H., and Kodama, T. Four new electrophoretically slow-moving glucose 6-phosphate dehydrogenase variants associated with congenital nonspherocytic hemolytic anemia found in Japan: Gd(-) Kurume, Gd(-) Fukushima, Gd(-) Yamaguchi and Gd(-) Wakayama. Am.J.Hematol. 5:131-138, 1978. * Miwa, S., Fujii, H., Nakashima, K., Miura, Y., Yaamada, K., Hagiwara, T., and Fukuda, M. Three new electrophoretically normal glucose-6-phosphate dehydrogenase variants associated with congenital nonspherocytic hemolytic anemia found in Japan: G6PD Ogikubo, Yokohama, and Akita. Hum.Genet. 45:11-17, 1978. * Morelli, A., Benatti, U., Gaetani, G.F., and De Flora, A. Biochemical mechanisms of glucose-6-phosphate dehydrogenase deficiency. Proc.Natl.Acad.Sci.USA 75:1979-1983, 1978. * North, M.L., Kahn, A., Boilletot, A., Bergerat, J.P., and Oberling, F. Un cas de deficit en glucose-6-phosphate deshydrogenase (Gd) "Seattle" dans une famille Alsacienne. La Nouv.Presse med. 7:1954-55, 1978. * Sicard, D., Kaplan, J.C., and Labie, D. Haemoglobinopathies and G-6-PD deficiency in Laos. Lancet 2:571-572, 1978. * Spielberg, S.P., Boxer, L.A., Corash, L.M., and Schulman, J.D. Improved erythrocyte survival with high dose vitamin E in chronic hemolyzing G6PD and glutathione synthetase deficiencies. Ann.Intern.Med. 90:53-54, 1978. * Stockman, J.A., Lubin, B., and Oski, A. Aspirin-induced hemolysis:The role of concomitant oxidant (H2O2) challenge. Pediatr.Res. 12:927-931, 1978. * Tokarev, Y.N., Chernyak, N.B., Batishchev, A.I., Lamzina,

N.V., and Alexeyev, G.A. tude des proprietes electrophoretiques et cinetiques de la glucose-6-phosphate deshydrogenase (Gd) d'erythrocytes dans les deficits hereditaires de l'enzyme. Description d'une nouvelle variante de glucose-6-phosphate deshydrogenase: la Gd Kremenchug. Nouv.Rev.Fr.Hematol. 20:557-564, 1978. * Wasserzug, O., Szeinberg, A., and Sperling, O. Erythrocyte glutathione reductase in gout and in glucose-6-phosphate dehydrogenase deficiency. Monogr.Hum.Genet. 9:16-19, 1978. * Welch, S.G., McGregor, I.A., and Williams, K. A new variant of human erythrocyte G6PD occurring at a high frequency amongst the population of two villages in the Gambia, West Africa. Hum.Genet. 40:305-309, 1978. * Welch, S.G., Lee, J., McGregor, I.A., and Williams, K. Red cell glucose 6 phosphate dehydrogenase genotypes of the population of two west African villages. Hum.Genet. 43:315-320, 1978. * Wiggans, R.G., Jacobson, R.J., Fialkow, P.J., Woolley, P.V., MacDonald, J.S., and Schein, P.S. Probable clonal origin of acute myeloblastic leukemia following radiation and chemotherapy of colon cancer. Blood 52:659-663, 1978. * Yamamura, K., Ogita, Z., and Miwa, S. Utilization of hair bulbs for the detection of heterozygotes of the electrophoretic G6PD variant. Jpn.J.Human Genet. 12:371-375, 1978. * Yoshida, A. and Beutler, E. Human glucose-6-phosphate dehydrogenase variants: A supplementary tabulation. Ann.Hum.Genet. 41:347-355, 1978. Notes: (B511). * Afolayan, A. Plasma membrane of human erythrocyte with different levels of glucose-6-phosphate dehydrogenase. Int.J.Biochem. 10:361-365, 1979. * Allen, L.C. Assay of erythrocyte glucose-6-phosphate dehydrogenase on the gemsaec analyser. Clin.Biochem. 12:179-181, 1979. * Bellini, T., Signorini, M., Dallocchio, F., and Rippa, M. Affinity labelling of the NADP+-binding site of glucose 6-phosphate dehydrogenase from Candida utilis. Biochem.J. 183:297-302, 1979. * Beutler, E., Blume, K.G., Kaplan, J.C., Lhr, G.W., Ramot, B., and Valentine, W.N. International committee for standardization in haematology: Recommended screening test for glucose-6-phosphate dehydrogenase (G-6-PD) deficiency. Br.J.Haematol. 43:465-476, 1979. Notes: (B554). * Beutler, E., West, C., and Johnson, C. Involvement of the erythroid series in acute myeloid leukemia. Blood 53:1203-1205, 1979. Notes: (B538). * Filippi, G., Rinaldi, A., Crisponi, G., Daniels, G.L., and Siniscalco, M. X-mapping in man: Evidence against measurable linkage between anhidrotic ectodermal dysplasia and G6PD deficiency. J.Med.Genet. 16:223-226, 1979. * Garcia, S.C., Moragon, A.C., and Lopez-Fernandez, M.E. Frequency of glutathione reductase, pyruvate kinase and glucose-6-phosphate dehydrogenase deficiency in a Spanish population. Hum.Hered. 29:310-313, 1979. * Gibbs, W.N., Gray, R., and Lowry, M. Glucose-6-phosphate dehydrogenase deficiency and neonatal jaundice in Jamaica. Br.J.Haematol. 43:263-274, 1979. * Hanel, H.K., Mejer, J., and Morck, H.I. Erythrocyte and

leucocyte enzymes in a case of paroxysmal nocturnal haemoglobinuria. Scand.J.Haematol. 22:253-257, 1979. * Heller, P., Best, W.R., Nelson, R.B., and Becktel, J. Clinical implications of sickle-cell trait and glucose-6-phosphate dehydrogenase deficiency in hospitalized black male patients. N.Engl.J.Med. 300:1001-1005, 1979. * Honig, G.R., Habacon, E., Vida, L.N., Matsumoto, F., and Beutler, E. Three new variants of glucose-6-phosphate dehydrogenase associated with chronic nonspherocytic hemolytic anemia: G-6-PD Lincoln Park, G-6-PD Arlington Heights, and G-6-PD West Town.. Am.J.Hematol. 6:353-360, 1979. Notes: (B546). * Johnson, G.J., Allen, D.W., Cadman, S., Fairbanks, V.F., White, J.G., Lampkin, B.C., and Kaplan, M.E. Red-cell-membrane polypeptide aggregates in glucose-6-phosphate dehydrogenase mutants with chronic hemolytic disease. N.Engl.J.Med. 301:522-527, 1979. * Kidder, W.R. and Beutler, E. Unpublished , 1979. Notes: G6PD Santa Barbara. * Kinugasa, A., Kusunoki, T., and Iwashima, A. Deficiency of glucose-6-phosphate dehydrogenase found in a case of hepatic fructose-1,6-diphosphatase deficiency. Pediatr.Res. 13:1361-1364, 1979. * Lapenson, D. and Deal, W.C.,Jr. Novel pronounced reversible inhibition of phosphofructokinase, glucose 6-phosphate dehydrogenase, and phosphoglucose isomerase by hexacyanoferrate (II). Arch.Biochem.Biophys. 193:521-528, 1979. * Levy, R. Glucose-6-phosphate dehydrogenases. Adv.Enzymol. 48:97-192, 1979. * Little, C. and Schacter, B. Hemolytic anemia following isobutyl nitrate (IBN) inhalation in a patient with glucose-6-phosphate dehydrogenase (G-6-PD) deficiency. Blood 54(Suppl.1):34A, 1979. * Luzzatto, L. Genetics of red cells and susceptibility to malaria. Blood 54:961-976, 1979. * Luzzatto, L. and Bienzle, U. The malaria/G-6-PD hypothesis. Lancet 1:1183-1184, 1979. * Luzzatto, L., Usanga, E.A., Bienzle, U., Esan, G.F.J., and Fasuan, F.A. Imbalance in X-chromosome expression: Evidence for a human x-linked gene affecting growth of hemopoietic cells. Science 205:1418-1420, 1979. * Manfredi, G., De Panfilis, G., Zampetti, M., and Allegra, F. Studies on dapsone induced haemolytic anaemia. I. Methaemoglobin production and G-6-PD activity in correlation with dapsone dosage. Br.J.Dermatol. 100:427-432, 1979. * Martin, S.K., Miller, L.H., Alling, D., Okoye, V.C., Esan, G.J.F., Osunkoya, B.O., and Deane, M. Severe malaria and glucose-6-phosphate-dehydrogenase deficiency: A reappraisal of the malaria/G-6-PD hypothesis. Lancet 1:524-526, 1979. * Milone, S., Massone, L., and Biocca, A. Screening of the G-6-PD deficiency in a sample of the Abruzzi population. Quad.Sclavo.Diagn. 15:845-850, 1979. Notes: The modified *Beutler* test has afterwards been employed for a screening research on 393 living in the Abruzzi subjects: none of them appeared to be affected by the G-6-PD defect. * Modiano, G., Battistuzzi, G., Esan, G.J.F., Testa, U., and Luzzatto, L. Genetic heterogeneity of "normal" human erythrocyte glucose-6-phosphate dehydrogenase: An isoelectrophoretic polymorphism. Proc.Natl.Acad.Sci.USA 76:852-856, 1979. * Morelli, A., Benatti, U., Salamino, F., Sparatore, B.,

Michetti, M., Melloni, E., Pontremoli, S., and De Flora, A. In vitro correction of erythrocyte glucose 6-phosphate dehydrogenase (G6PD) deficiency. Arch.Biochem.Biophys. 197:543-550, 1979. * Nakatsuji, T. and Miwa, S. Incidence and characteristics of glucose-6-phosphate dehydrogenase variants in Japan. Hum.Genet. 51:297-305, 1979. Notes: G6PD Konan, Kamiube and Kiwa. * Newman, J.G., Newman, T.B., Bowie, L.J., and Mendelsohn, J. An examination of the role of vitamin E in glucose-6-phosphate dehydrogenase deficiency. Clin.Biochem. 12:149-151, 1979. * Oluboyede, O.A., Esan, G.J.F., Francis, T.I., and Luzzatto, L. Genetically determined deficiency of glucose 6-phosphate dehydrogenase (type A-) is expressed in the liver. J.Lab.Clin.Med. 93:783-789, 1979. * Prchal, J., Moreno, H., Conrad, M., and Vitek, A. G-6-PD Dothan: A new variant associated with chronic hemolytic anemia. IRCS 7:348, 1979. * Talukder, G. and Sharma, A. Genetic diseases in India-present status. Proc.Indian Natn.Sci.Acad. 45:273-301, 1979. * Thomas, W.A., Reiner, J.M., Janakidevi, K., Florentin, R.A., and Lee, K.T. Population dynamics of arterial cells during atherogenesis. Exp.Mol.Pathol. 31:367-386, 1979. * Veglio, V. and Gaiottino, F. Crisi emolitica da deficit di G-6-PD in corso di epatite virale di tipo a. Minerva Med. 70:357-360, 1979. * Vergnes, H. and Brun, H. Characterization of some erythrocyte G6PD variants by isoelectric focusing. Hum.Genet. 53:43-45, 1979. * Vergnes, H., Gherardi, M., Lefevre-Witier, P.H., Jaeger, G., and Benabadji, M. Genetic variants of human glucose-6-phosphate dehydrogenase in a Saharian and pygmy family. Hum.Hered. 29:50-56, 1979. Notes: A description of G 6 PD Ibadan. * Vergnes, H. Isoelectric focusing of human G6PD on thin-layer polyacrylamide gel. Science Tools 26:67-70, 1979. * Winterbourn, C.C. Protection by ascorbate against acetylphenylhydrazine-induced Heinz body formation in glucose-6-phosphate dehydrogenase deficient erythrocytes. Br.J.Haematol. 41:245-252, 1979. * Bernstein, S.C., Bowman, J.E., and Noche, L.K. Population studies in Cameroon. Hum.Hered. 30:251-258, 1980. * Bernstein, S.C., Bowman, J.E., and Noche, L.K. Genetic variation in Cameroon: Thermostability variants of hemoglobin and of glucose-6-phosphate dehydrogenase. Biochem.Genet. 18:21-37, 1980. * Beutler, E. G 6 PD as a genetic marker. Hemoglobin 4:761-767, 1980. Notes: (B588). * Bianchine, J.R. and Lubbers, J.R. Human investigation of chronic chlorite ingestion by glucose-6-phosphate dehydrogenase deficient males. Clin.Res. 28:816A, 1980. * Boon, W.H. Singapore kernicterus. Singapore Med.J. 21:556-567, 1980. * Calvert, A.F. and Trimble, G.E. Glucose-6-phosphate dehydrogenase in an Afro-American population. Hum.Hered. 30:271-277, 1980. * Chockkalingam, K. and Board, P.G. Further evidence for heterogeneity of glucose-6-phosphate dehydrogenase deficiency in Papua New Guinea. Hum.Genet. 56:209-212, 1980. * Corash, L., Spielberg, S., Bartsocas, C., Boxer, L.,

Steinherz, R., Sheetz, M., Egan, M., Schlessleman, J., and Schulman, J.D. Reduced chronic hemolysis during high-dose vitamin E administration in Mediterranean-type glucose-6-phosphate dehydrogenase deficiency. N.Engl.J.Med. 303:416-420, 1980. * D'Urso, M., Battistuzzi, G., and Luzzatto, L. Genetic variants of human erythrocyte glucose 6-phosphate dehydrogenase: Automated procedure for characterization by column chromatography. Anal.Biochem. 108:146-150, 1980. * Damiani, G., Frascio, M., Benatti, U., Morelli, A., Zocchi, E., Fabbi, M., Bargellesi, A., Pontremoli, S., and De Flora, A. Monoclonal antibodies to human erythrocyte glucose 6-phosphate dehydrogenase. FEBS Lett. 119:169-173, 1980. * Fairbanks, V.F., Nepo, A.G., Beutler, E., Dickson, E.R., and Honig, G. Glucose-6-phosphate dehydrogenase variants: Reexamination of G6PD Chicago and Cornell and a new variant (G6PD Pea Ridge) resembling G6PD Chicago. Blood 55:216-220, 1980. Notes: (B561). * Gahr, M. Isoelectric focusing of hexokinase and glucose-6-phosphate dehydrogenase isoenzymes in erythrocytes of newborn infants and adults. Br.J.Haematol. 46:529-535, 1980. * Gealy, W.J., Dwyer, J.M., and Harley, J.B. Allelic exclusion of glucose-6-phosphate dehydrogenase in platelets and T lymphocytes from a Wiskott-Aldrich syndrome carrier. Lancet 1:63-65, 1980. * Gibbs, W.N., Wardle, J., and Serjeant, G.R. Glucose-6-phosphate dehydrogenase deficiency and homozygous sickle cell disease in Jamaica. Br.J.Haematol. 45:73-80, 1980. * Gloria-Bottini, F., Falsi, A.M., Mortera, J., and Bottini, E. The relations between G-6-PD deficiency, thalassemia and malaria. Further analysis of data from Sardinia and the Po valley. Experientia 36:541-543, 1980. * Gonzalez, R., Estrada, M., Garcia, M., and Gutierrez, A. G6PD Ciudad de la Habana: A new slow variant with deficiency found in a Cuban family. Hum.Genet. 55:133-135, 1980. * Hitzeroth, H.W. and Bender, K. Erythrocyte G-6-PD and 6-PGD genetic polymorphisms in South African negroes, with a note on G-6-PD and the malaria hypothesis. Hum.Genet. 54:233-242, 1980. * Jansson, S., Hekali, R., Gripenberg, J., Haorkoenen, M., and Vuopio, P. Membrane characteristics and metabolic properties of glucose-6-phosphate dehydrogenase deficient red cells. Br.J.Haematol. 46:79-87, 1980. * Johnson, G.J. and Beutler, E. Unpublished , 1980. Notes: Patient name - Terry Johnson. * Kirkman, H.N., Wilson, W.G., and Clemons, E.H. Regulation of glucose-6-phosphate dehydrogenase. J.Lab.Clin.Med. 95:877-887, 1980. * Lagrange, J.L., Marie, J., Cottreau, D., Fischer, S., and Kahn, A. Endogenous phosphorylation of soluble enzymes in human red cells. Biochim.Biophys.Acta 612:213-225, 1980. * Lucotte, G. Polymorphisme eletrophoretique des proteines et enzymes seriques et erythrocytaires chez le Chimpanze. Hum.Genet. 54:97-102, 1980. * Martin, P.J., Najfeld, V., Hansen, J.A., Penfold, G.K., Jacobson, R.J., and Fialkow, P.J. Involvement of the B-lymphoid system in chronic myelogenous leukaemia. Nature 287:49-50, 1980. * Martin, S.K. Modified G-6-PD/malaria hypothesis. Lancet 1:51, 1980. * McCann, S.R., Smithwick, A.M., Temperley, I.J., and Tipton, K. G6PD (Dublin): Chronic non-spherocytic haemolytic anaemia resulting from glucose-6-phosphate dehydrogenase deficiency in

an Irish kindred. J.Med.Genet. 17:191-193, 1980. * Meloni, T., Corti, R., Costa, S., Mele, G., and Franca, V. Alpha-thalassaemia and hyperbilirubinaemia in G-6-PD-deficient newborns. Arch.Dis.Child. 55:482-484, 1980. * Mentzer, W.C.J., Warner, R., Addiego, J., Smith, B., and Walter, T. G6PD San Francisco: A new variant of glucose-6-phosphate dehydrogenase associated with congenital nonspherocytic hemolytic anemia. Blood 55:195-198, 1980. Notes: A G6PD variant that is inactivated by dialysis and reactivatd by high contrations of Mg and NADP. * Miwa, S. Clinical and biochemical studies on mutant red cell enzymes mainly associated with hemolytic anemia. Jpn.J.Human Genet. 25:83-92, 1980. * Panich, V., Bumrungtrakul, P., Jitjai, C., Kamolmatayalkul, S., Khoprasert, B., Klaisuvan, C., Kongmuang, U., Maneechai, P., Pornpatkul, M., Ruengrairatanaroje, P., Piyarat, S., and Viriyayudhakorn, S. Glucose-6-phosphate dehydrogenase deficiency in South Vietnamese. Hum.Hered. 30:361-364, 1980. * Panich, V. and Na-Nakorn, S. G 6 PD deficiency in senile cataracts. Hum.Genet. 55:123-124, 1980. * Panich, V. and Na-Nakorn, S. G-6-PD variants in Thailand. J.Med.Assoc.Thai. 63:537-543, 1980. * Panich, V., Na-Nakorn, S., and Wasi, P. G-6-PD variants in Chinese in Thailand. Southeast Asian J.Trop.Med.Public Health 11:250-255, 1980. * Panich, V. Glucose-6-phosphate dehydrogenase in Thailand. Hum.Genet. 53:227-228, 1980. * Picat, C., Etiemble, J., Boivin, P., and Le Prise, P.Y. Gd(-) Rennes a new deficient variant of glucose-6-phosphate dehydrogenase associated with congenital nonspherocytic hemolytic anemia found in France. Hum.Genet. 55:125-127, 1980. * Prchal, J.T., Crist, W.M., Malluh, A., Vitek, A., Tauxe, W.N., and Carroll, A.J. A new glucose-6-phosphate dehydrogenase deficient variant in a patient with Chediak-Higashi Syndrome. Blood 56:476-480, 1980. Notes: G 6 PD Birmingham. * Prchal, J.T., Carroll, A.J., Prchal, J.F., Crist, W.M., Skalka, H.W., Gealy, W.J., Harley, J., and Mulluh, A. Wiscott-Aldrich Syndrome: Cellular impairments and their implication for carrier detection. Blood 56:1048-1054, 1980. * Rostand, S.G., Culpepper, R.M., and Prchal, J.T. Urinary acidification in a patient with glucose-6-phosphate dehydrogenase deficiency. Am.J.Med. 69:155-158, 1980. * Sanna, G., Frau, F., Melis, M.A., Galanello, R., De Virgiliis, S., and Cao, A. Interaction between the glucose-6-phosphate dehydrogenase deficiency and thalassaemia genes at phenotype level. Br.J.Haematol. 44:555-561, 1980. * Sazama, K., Klein, H.G., Davey, R.J., and Corash, L. Intraoperative hemolysis. Arch.Intern.Med. 140:845-846, 1980. * Shatskaya, T.L., Krasnopolskaya, K.D., Tzoneva, M., Mavrudieva, M., and Toncheva, D. Variants of erythrocyte glucose-6-phosphate dehydrogenase (G6PD) in Bulgarian populations. Hum.Genet. 54:115-117, 1980. * Shatskaya, T.L., Krasnopolskaya, K.D., and Zakharova, T.V. Regularities of distribution of Gd- alleles in Azerbaijan. III. Identification of G 6 PD mutant forms. Genetika 16:2217-2225, 1980. * Sidi, Y., Aderka, D., Brok-Simoni, F., Benajmin, D., Ramot, B., and Pinkhas, J. Viral hepatitis with extreme hyperbilirubinemia, massive hemolysis and encephalopathy in a

patient with a new G 6 PD variant. Isr.J.Med.Sci. 16:130-133, 1980. * Testa, U., Meloni, T., Lania, A., Battistuzzi, G., Cutillo, S., and Luzzatto, L. Genetic heterogeneity of glucose 6-phosphate dehydrogenase deficiency in Sardinia. Hum.Genet. 56:99-105, 1980. * Travis, S.F., Kumar, S.P., Paez, P.C., and Delivoria-Papadopoulos, M. Red cell metabolic alterations in postnatal life in term infants: Glycolytic enzymes and glucose-6-phosphate dehydrogenase. Pediatr.Res. 14:1349-1352, 1980. * Tzortzatou-Stathopolou, F., Zannos-Mariolea, L., Karayiannis, P., Constantsas, N., and Matsaniotis, N. Leucocyte glucose-6-phosphate dehydrogenase (G-6-PD) activity in G-6-PD deficient subjects. Eur.J.Pediatr. 135:37-39, 1980. * Vives-Corrons, J.L., Pujades, A., and Curia, M.D. Caracterizacion molecular de la glucosa-6-fosfato deshidrogenasa (G6PD) en 24 casos de deficit enzimatico y descripcion de una nueva variante (G6PD-Betica). Sangre (Barc.) 25:1049-1064, 1980. * Vives-Corrons, J.L. and Pujades, M.A. Heterogeneity of "Mediterranean-type" glucose-6-phosphate dehydrogenase (G6PD) deficiency in Spain and description of two new variants associated with favism. Hum.Genet. 60:216-221, 1980. * Westerman, M.P., Wald, N., and Diloy-Puray, M. Irradiation shortens the survival time of red cells deficient in glucose-6-phosphate dehydrogenase. Radiat.Res. 81:473-477, 1980. * Williamson, D. and Winterbourn, C.C. Effect of oral administration of ascorbate on acetylphenylhydrazine-induced Heinz body formation. Br.J.Haematol. 46:319-321, 1980. * Wilson, W.G., Kirkman, H.N., and Clemons, E.H. Regulation of glucose-6-phosphate dehydrogenase. II. Resealed red cell ghosts. J.Lab.Clin.Med. 95:888-896, 1980. * Anonymous What antipyretics and analgesics, and in what dosage, are safe for general use in children suffering from glucose-6-phosphate dehydrogenase deficiency? Is paracetamol safe in these circumstances? BMJ 282:2041, 1981. * Arnold, H., Lhr, G.W., Hasslinger, K., and Ludwig, R. Combined erythrocyte glucosephosphate isomerase (GPI) and glucose-6-phosphate dehydrogenase (G6PD) deficiency in an Italian family. Hum.Genet. 57:226-229, 1981. * Bleiber, R., Eggert, W., Reichmann, G., and Kunze, D. Phospholipid content and phospholipid fatty acid composition of red blood cells in enzyme defect hemolytic anemias. Acta Biol.Med.Ger. 40:1133-1138, 1981. * Brown, P.J. New considerations on the distribution of malaria, thalassemia, and glucose-6-phosphate dehydrogenase deficiency in Sardinia. Hum.Biol. 53:367-382, 1981. * Camardella, L., Romano, M., Di Prisco, G., and Descalzi-Cancedda, F. Human erythrocytes glucose-6-phosphate dehydrogenase: Labelling of a reactive lysyl residue by pyridoxal-5'-phosphate. Biochem.Biophys.Res.Commun. 103:1384-1389, 1981. * Chuanshu, D., Yankang, X., Lin, W.Q.R., and Xiaoyun, H. Studies on erythrocyte glucose-6-phosphate dehydrogenase variants in Chinese. I. Gd(-) Liau-Baisha. Acta Academiae Medicinae Zhong 2:649-658, 1981. * Colonna, P. Aspirin and glucose-6-phosphate dehydrogenase deficiency. BMJ 283:1189, 1981. * De Flora, A., Morelli, A., Benatti, U., Giuntini, P., Ferraris, A.M., Galiano, S., Ravazzolo, R., and Gaetani, G.F. G6PD Napoli and Ferrara II: Two new glucose-6-phosphate

dehydrogenase variants having similar characteristics but different intracellular lability and specific activity. Br.J.Haematol. 48:417-423, 1981. * Ferraris, A.M., Giuntini, P., Galiano, S., and Gaetani, G.F. 2-Deoxy-glucose-6-phosphate utilization in the study of glucose-6-phosphate dehydrogenase mosaicism. Am.J.Hum.Genet. 33:307-313, 1981. * Fujii, H., Miwa, S., Tani, K., Takegawa, S., Fujinami, N., Takahashi, K., Nakayama, S., Konno, M., and Sato, T. Glucose-6-phosphate dehydrogenase variants: A unique variant (G6PD Kobe) showed an extremely increased affinity for galactose 6-phosphate and a new variant (G6PD Sapporo) resembling G6PD Pea Ridge. Hum.Genet. 58:405-407, 1981. * Ghosh, U., Banerjee, T., Banerjee, P.K., and Saha, N. Distribution of haemoglobin and glucose-6-phosphate dehydrogenase phenotypes among different caste groups of Bengal. Hum.Hered. 31:119-121, 1981. * Hitzeroth, H.W. and Bender, K. Age-dependency of somatic selection in South African negro G-6-PD heterozygotes. Hum.Genet. 58:338-343, 1981. * Khoo, K.K. The treatment of malaria in glucose-6-phosphate dehydrogenase. Ann.Trop.Med.Parasitol. 75:591-5, 1981. * Kratzer, P.G. and Chapman, V.M. X chromosome reactivation in oocytes of mus caroli. Proc.Natl.Acad.Sci.USA 78:3093-3097, 1981. * Magon, A.M., Leipzig, R.M., Zannoni, V.G., and Brewer, G.J. Interactions of glucose-6-phosphate dehydrogenase deficiency with drug acetylation and hydroxylation reactions. J.Lab.Clin.Med. 97:764-770, 1981. * Marx, J.L. Natriuretic hormone linked to hypertension. Science 212:1255-1257, 1981. * Matthay, K.K. and Mentzer, W.C. Erythrocyte enzymopathies in the newborn. Clin.Haematol. 10:31-55, 1981. * Migeon, B.R., Moser, H.W., Moser, A.B., Axelman, J., Sillence, D., and Norum, R.A. Adrenoleukodystrophy: evidence for x linkage, inactivation, and selection favoring the mutant allele in heterozygous cells. Proc.Natl.Acad.Sci.USA 8:5066-5070, 1981. Notes: Skin fibroblasts of human males affected with adrenoleukodystrophy (ALD) have previously been shown to be abnormal with respect to C26 fatty acid content. Skin fibroblast clones from heterozygotes in three families segregating this mutation have been analyzed and are of two types: clones with normal ratios of C26 to C22 fatty acids and clones with an excess of C26 fatty acids similar to that found in cells of affected males. This indicates not only that the locus is X linked but also that it is subject to inactivation. In most of the heterozygotes there were significantly more clones of abnormal type than those expressing the normal allele, indicating a proliferative advantage in vitro for skin fibroblasts of mutant type. The increased levels of fatty acids in plasma in most heterozygotes and the phenotype of blood cells of women heterozygous for both ALD and glucose-6-phosphate dehydrogenase (G6PD) in one family are evidence that selection favoring the mutant allele may occur in vivo as well as in * Morelli, A., Benatti, U., Lenzerini, L., Sparatore, B., Salamino, F., Melloni, E., Michetti, M., Pontremoli, S., and De Flora, A. The interference of leukocytes and platelets with the measurement of glucose 6-phosphate dehydrogenase activity of erythrocytes with low activity variants of the enzyme. Blood 58:642-644, 1981.

* Nakatsuji, T. and Miwa, S. A new improved electrophoretic method of glucose-6-phosphate dehydrogenase with discontinuous buffer and gel system. Anal.Biochem. 112:52-54, 1981. * Nsouly, G.M. and Prchal, J.T. Characterization of a new G6PD variant and its associated oxidative damage. Clin.Res. 29:829, 1981. * Orzalesi, N., Sorcinelli, R., and Guiso, G. Increased incidence of cataract in male subjects deficient in glucose-6-phosphate dehydrogenase. Arch.Ophthalmol. 99:69-70, 1981. * Persico, M.G., Toniolo, D., Nobile, C., D'Urso, M., and Luzzatto, L. cDNA sequences of human glucose 6-phosphate dehydrogenase cloned in pBR322. Nature 294:778-780, 1981. * Ponnampalam, J.T. Haemoglobinuria after a single dose treatment with dapsone and pyrimethamine for falciparum malaria in a patient with glucose-6-phosphate dehydrogenase deficiency. Trop.Geogr.Med. 33:401-2, 1981. * Saha, N. and Patgunarajah, N. Phenotypic and quantitative relationship of red cell acid phosphatase with haemoglobin, haptoglobin, and G6PD phenotypes. J.Med.Genet. 18:271-275, 1981. * Samuel, A.P.W., Saha, N., Omer, A., and Hoffbrand, A.V. Quantitative expression of G6PD activity of different phenotypes of G6PD and haemoglobin in a Sudanese population. Hum.Hered. 31:110-115, 1981. * Sansone, G., Perroni, L., Testa, U., Mareni, C., and Luzzatto, L. New genetic variants of glucose-6-phosphate dehydrogenase (G6PD) in Italy. Ann.Hum.Genet. 45:97-104, 1981. * Seth, P.K., Devi, S.T., and Seth, S. Glucose-6-phosphate dehydrogenase deficiency and mental retardation. J.Inherit.Metab.Dis. 4:93-94, 1981. * Smith, J.W. and Beutler, E. Unpublished , 1981. Notes: G 6 PD Linda Vista. Patient-- Nouthong Souksamlane/G 6 PD Laos. Patient-- Phitsanoo Kanh. * Tan, K.L. Glucose-6-phosphate dehydrogenase status and neonatal jaundice. Arch.Dis.Child. 56:874-877, 1981. * Weimer, T.A., Salzano, F.M., and Hutz, M.H. Erythrocyte isozymes and hemoglobin types in a southern Brazilian population. J.Hum.Evolution 10:319-328, 1981. Notes: G 6 PD "Guaiba", characterized only by electrophoretic mobility. * Willcox, M.C. and Beckman, L. Haemoglobin variants, beta-thalassaemia and G-6-PD types in Liberia. Hum.Hered. 31:339-347, 1981. * Yermakov, N., Tokarev, J., Chernjak, N., Schoenian, G., Grieger, M., Guckler, G., Jacobasch, G., Mahmudova, M., and Bahramov, S. New stable mutant Gd(-) variants: G6PD Tashkent and G6PD Nucus. Molecular basis of hereditary enzyme deficiency. Acta Biol.Med.Ger. 40:559-562, 1981. * Bapat, J.P. and Baxi, A.J. Mechanism of hemolysis of G-6-PD deficient red cells: Changes in membrane lipids and polypeptides. Blut 44:355-362, 1982. * Bartsocas, C.S., Schulman, J.D., and Corash, L. Can acetaminophen cause hemolysis in G6PD deficiency? Acta Haematol.(Basel) 67:228, 1982. * Beutler, B.A., Stefansson, K., and Arnason, B.G.W. A biochemically distinct sub-population of neurons in the human substantia gelatinosa. Study with G-6-PD histochemistry. J.Neurol.Sci. 55:175-183, 1982. * Beutler, E. and Taylor, G.P. Unpublished , 1982. Notes: G 6 PD Mercury. Patient-- McNeal.

* Beutler, E. G-6-PD: Historical perspective and current status. In: Advances in Red Blood Cell Biology, edited by Weatherall, D.J., Fiorelli, G., and Gorini, S.New York:Raven Press, 1982,p. 297-308. Notes: (B609). * Casassus, P., Vannetzel, J.M., and Lortholary, P. Hemolyse aigue par deficit en glucose 6 phosphate deshydrogenase au debut du traitement d'un myelome role du melphalan. Nouv.Presse Med. 11:2296, 1982. * Chockkalingam, K., Board, P.G., and Nurse, G.T. Glucose-6-phosphate dehydrogenase deficiency in Papua New Guinea. The description of 13 new variants. Hum.Genet. 60:189-192, 1982. * Chockkalingam, K., Board, P.G., and Breguet, G. Glucose 6-phosphate dehydrogenase variants of Bali Island (Indonesia). Hum.Genet. 60:60-62, 1982. * Dao, M.L., Johnson, B.C., and Hartman, P.E. Preparation of a monoclonal antibody to rat liver glucose-6-phosphate dehydrogenase and the study of its immunoreactivity with native and inactivated enzyme. Proc.Natl.Acad.Sci.USA 79:2860-2864, 1982. * Deacon-Smith, R. The ascorbate cyanide test and the detection of females heterozygous for glucose-6-phosphate dehydrogenase deficiency. Med.Lab.Sci. 39:139-143, 1982. * Elizondo, J., Saenz, G.F., Paez, C.A., Ramon, M., Garcia, M., Gutierrez, A., and Estrada, M. G6PD-Puerto Limon: A new deficient variant of glucose-6-phosphate dehydrogenase associated with congenital nonspherocytic hemolytic anemia. Hum.Genet. 62:110-112, 1982. * Estrada, M., Garcia, M., Gutierrez, A., Quintero, I., and Gonzalez, R. G6PD Varadero. Vox Sang. 43:102-104, 1982. * Fenu, M.P., Finazzi, G., Manoussakis, C., Palomba, V., and Fiorelli, G. Glucose-6-phosphate dehydrogenase deficiency: Genetic heterogeneity in Sardinia. Ann.Hum.Genet. 46:105-114, 1982. * Gerli, G.C., Beretta, L., Bianchi, M., Agostoni, A., Gualandri, V., and Orsini, G.B. Erythrocyte superoxide dismutase, catalase and glutathione peroxidase in glucose-6-phosphate dehydrogenase deficiency. Scand.J.Haematol. 29:135-140, 1982. * Haghighi, B. and Levy, H.R. Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. Kinetics of reassociation and reactivation from inactive subunits. Biochemistry 21:6429-6434, 1982. Notes: Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides is denatured in 8 M urea and dissociated into its two inactive subunits. Denaturation leads to an approximately 80% decrease in protein fluorescence and a 20-nm red shift in the emission maximum. Upon dilution, the urea-treated enzyme regains catalytic activity (approximately 70%). The reactivated enzyme is indistinguishable from the native enzyme based on a number of physicochemical and enzymological criteria. The kinetics of renaturation and reactivation were monitored by measuring the rates of regain of native fluorescence and appearance of activity and the accessibility of histidine residues toward diethyl pyrocarbonate modification. Regain of native fluorescence was too rapid to measure at 25 degrees C; at 5 degrees C the initial phase was also too rapid, but a slower phase was monitored and shown to obey first-order kinetics with k = (5.9 +/- 1.3) x 10(-3) s-1. Reappearance of activity was measured at several protein concentratio * Hill, F.G.H. Haematological disorders.

Clin.Obstet.Gynaecol. 9:75-90, 1982. * Jackson, C.E., Cerny, J.C., Block, M.A., and Fialkow, P.J. Probable clonal origin of aldosteronomas versus multicellular origin of parathyroid adenomas. Surgery 92:875-879, 1982. * Kende, G., Ben-Bassat, I., Brok-Simoni, F., Holtzman, F., and Ramot, B. Adenylate kinase deficiency associated with congenital non-spherocytic hemolytic anemia. Abstr.XIX Int.Soc.Haematol. 19:224, 1982. * Kitao, T., Ito, K., Hattori, K., Matsuki, T., and Yoneyama, Y. G6PD Kanazawa: A new variant of glucose-6-phosphate dehydrogenase associated with congenital nonspherocytic hemolytic anemia. Acta Haematol.(Basel) 68:131-135, 1982. * Krasnopolskaia, K.D. and Bochkov, N.P. Genetic heterogeneity of hereditary enzymopathies. Vestn.Akad.Med.Nauk.SSSR 9:56-64, 1982. * Meloni, T., Corti, R., Naitana, A.F., and Arese, P. Lack of effect of phototherapy on red cell riboflavin status and on glucose-6-phosphate dehydrogenase activity in normal and G-6-PD-deficient subjects with neonatal jaundice. J.Pediatr. 100:972-974, 1982. * Panich, V. Glucose-6-phosphate dehydrogenase deficiency: Genetic heterogeneity in Asia. In: Advances in Red Blood Cell Biology,Anonymous New York:Raven Press, 1982,p. 329-338. * Perroni, L., Tassara, P., Baldi, M., Reali, R., and Scartezzini, P. G 6 PD variants detected in Genoa area. In: Advances in Red Blood Cell Biology, edited by Weatherall, D.J., Fiorelli, G., and Gorini, S.New York:Raven Press, Inc. 1982,p. 409-416. * Persico, M., Battistuzzi, G., Mareni, C., Nobile, C., D'Urso, M., Toniolo, D., and Luzzatto, L. Genetic variants of human glucose-6-phosphate dehydrogenase (G6PD): Studies of turnover and of G6PD-specific mRNA. In: Advances in Red Blood Cell Biology, edited by Weatherall, D.J., Fiorelli, G., and Gorini, S.New York:Raven Press, 1982,p. 309-318. * Pirisi, L., Pascale, R., Daino, L., Frassetto, S., and La, S.V. Effect of glucose-6-phosphate dehydrogenase deficiency on the benz(a)pyrene toxicity for in vitro cultured human skin fibroblasts. Res.Commun.Chem.Pathol.Pharmacol. 38:301-11, 1982. * Shannon, K. and Buchanan, G.R. Severe hemolytic anemia in black children with glucose-6-phosphate dehydrogenase deficiency. Pediatrics 70:364-369, 1982. * Spangenberg, P., Bosia, A., Arese, P., Losche, W., and Till, U. Comparative studies on human blood platelets of normal and glucose-6-phosphate-dehydrogenase-deficient donors. Acta Biol.Med.Ger. 41:25-31, 1982. * Takahashi, K., Fujii, H., Takegawa, S., Tani, K., Hirono, A., Takizawa, T., Kawakatsu, T., and Miwa, S. A new glucose-6-phosphate dehydrogenase variant (G6PD Nagano) associated with congenital hemolytic anemia. Hum.Genet. 62:368-370, 1982. * Toncheva, D., Evres, T., and Tzoneva, M. G6PD in immature and mature human brain: Electrophoretic and enzyme kinetic studies. Hum.Hered. 32:193-196, 1982. * Vaca, G., Ibarra, B., Romero, F., Olivares, N., Cantu, J.M., and Beutler, E. G-6-PD Guadalajara: A new mutant associated with chronic non-spherocytic hemolytic anemia. Hum.Genet. 61:175-176, 1982. Notes: (B630) Patient-- Genero Rodriquez. * Vives-Corrons, J.L., Feliu, E., Pujades, M.A., Rozman, C., Carreras, A., and Vallespi, M.T. Severe glucose-6-phosphate

dehydrogenase (G 6 PD) deficiency associated with chronic hemolytic anemia, granulocyte dysfunction and increased susceptibility to infections. Description of a new molecular variant (G 6 PD Barcelona). Blood 59:428-434, 1982. * Vives-Corrons, J.L. and Pujades, A. Heterogeneity of Mediterranean type glucose-6-phosphate dehydrogenase (G-6-PD) deficiency in Spain and description of two new variants associated with Favism. Hum.Genet. 60:216-221, 1982. * Wijnen, J.T., Rijken, H., deBoer, L.E.M., and Khan, P.M. Glucose-6-phosphate dehydrogenase (G6PD) variation in the orang utan. In: The Orang Utan. Its Biology and Conservation, edited by deBoer, L.E.M.The Hague:Dr. W. Junk, 1982,p. 109-118. * Woolhouse, N.M. and Atu-Taylor, L.C. Influence of double genetic polymorphism on response to sulfamethazine. Clin.Pharmacol.Ther. 31:377-383, 1982. * Zampella, E.J., Bradley, E.L., and Pretlow, T.G. Glucose-6-phosphate dehydrogenase A possible clinical indicator for prostatic carcinoma. Cancer 49:384-387, 1982. * Adams, M.J., Levy, H.R., and Moffat, K. Crystallization and preliminary X-ray data for glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. J.Biol.Chem. 258:5867-5868, 1983. * Ashkenazi, S., Mimouni, F., Merlob, P., and Reisner, S.H. Neonatal bilirubin levels and glucose-6-phosphate dehydrogenase deficiency in preterm and low-birth weight infants in Israel. Isr.J.Med.Sci. 19:1056, 1983. * Baird, J.K., Davidson, D.E., and Decker-Jackson, J.E. Oxidative activity of hydroxylated primaquine analogs: Non-toxicity to hemolytically sensitive red blood cells in vitro. Blood 62 Supplement 1:42a, 1983. * Beutler, E. Glucose-6-phosphate dehydrogenase deficiency. In: The Metabolic Basis of Inherited Disease, edited by Stanbury, J.B., Wyngaarden, J.B., Fredrickson, D.S., Goldstein, J.L., and Brown, M.S.New York:McGraw-Hill, Inc. 1983,p. 1629-1653. Notes: (B618). * Beutler, E. Glucose-6-phosphate dehydrogenase deficiency. In: Hematology, edited by Williams, W.J., Beutler, E., Erslev, A., and Lichtman, M.A.New York:McGraw-Hill, Inc. 1983,p. 561-574. Notes: (B659). * Beutler, E., Phyliky, R.L., and Nishimura, R.A. Unpublished , 1983. Notes: G 6 PD Fort Pierce. Patient-- Michael Autullo. * Beutler, E. Glucose-6-phosphate dehydrogenase deficiency in drug-induced hemolysis. In: Current Therapy in Hematology-Oncology 1983-1984, edited by Brain, M.C. and Mc Culloch, P.B.Philadelphia:B. C. Decker, Inc. 1983,p. 58-60. Notes: (B629). * Bloom, K.E., Brewer, G.J., Magon, A.M., and Wetterstroem, N. Microsomal incubation test of potentially hemolytic drugs for glucose-6-phosphate dehydrogenase deficiency. Clin.Pharmacol.Ther. 33:403-9, 1983. * Craney, C.L. and Goffredo, M.E. A rapid affinity chromatography procedure for the isolation of glucose-6-phosphate dehydrogenase from human erythrocytes. Anal.Biochem. 128:312-316, 1983. * Deneke, S.M., Gershoff, S.N., and Fanburg, B.L. Potentiation of oxygen toxicity in rats by dietary protein or amino acid deficiency. J.Appl.Physiol. 54:147-151, 1983. Notes: Rats fed 3% casein diets for 6 days showed an increased susceptibility to greater than 98% oxygen [mean survival time 46.9 +/-4.1 (SD) h] compared with animals fed 25% casein diets

(mean survival time 60 +/- 5 h). The 3% casein diet did not reduce the responses to hyperoxia of lung glucose-6-phosphate dehydrogenase, glutathione peroxidase, and glutathione reductase (NAD(P)H), which maintain tissue levels of reduced glutathione or lung superoxide dismutase levels. While supplementation of the 3% casein diet with the sulfur-containing amino acids (cysteine, cystine, or methionine) prevented the increased oxygen toxicity, supplementation with leucine, a nonsulfur-containing amino acid, had no effect on potentiation of toxicity. Animals fed the unsupplemented 3% casein diet failed to show an elevation of lung glutathione in response to hyperoxia. When the 3% casein diet was supplemented with cysteine, total lung glutathione levels increased normally during oxygen exposure. Supplementation of the 25% pro * Doll, D.C. Oxidative haemolysis after administration of doxorubicin. BMJ 287:180-181, 1983. * Ermakov, N.V., Chernyak, N.B., and Tokarev, Y.N. Properties of new variant of glucose-6-phosphate dehydrogenase (Regar variant). Glucose metabolism in erythrocytes containing abnormal enzyme. Biokhimiia 48:577-583, 1983. * Ferraris, A.M., Canepa, L., Marenia, C., Baule, G., Meloni, T., Salvidio, E., Forteleoni, G., and Gaetani, G.F. Reexpression of normal stem cells in erythroleukemia during remission. Blood 62:177-179, 1983. * Glader, B.E. and Backer, K. Diagnosis of red blood cell (RBC) pyruvate kinase (PK) deficiency in patients with normal enzyme activity. Blood 62 Supplement 1:46a, 1983. * Golenser, J., Miller, J., Spira, D.T., Navok, T., and Chevion, M. Inhibitory effect of a fava bean component on the in vitro development of Plasmodium falciparum in normal and glucose-6-phosphate dehydrogenase deficient erythrocytes. Blood 61:507-510, 1983. * Grieger, M. Medikamentos bedingte Hamolysen bei Patienten mit glukose-6-phosphat-dehydrogenase-Mangel. Folia Haematol.(Leipz.) 110:692-703, 1983. * Gualandri, V., Orsini, G.B., and Porta, E. Le deficit en glucose-6-phosphate deshydrogenase dans la population scolaire de Milan. J.Genet.Hum. 31:201-209, 1983. * Hsu, S., Luk, G.D., Krush, A.J., Hamilton, S.R., and Hoover Jr, H.H. Multiclonal origin of polyps in Gardner Syndrome. Science 221:951-953, 1983. * Jacobasch, G., Bleiber, R., and Schonian, G. Metabolism of the hexose monophosphate shunt in glucose-6-phosphate dehydrogenase deficiency and closely interrelated reactions. Haematologia (Budap) 15:401-407, 1983. * Johnson, G.J., Vatassery, G.T., Finkel, B., and Allen, D.W. High-dose vitamin E does not decrease the rate of chronic hemolysis in glucose-6-phosphate dehydrogenase deficiency. N.Engl.J.Med. 308:1014-1017, 1983. * Kasper, M., Miller, W., and Jacob, H. Immune complex guided red cell injury: A mechanism of infectious hemolysis. Blood 62 Supplement 1:47a, 1983. * Kennedy, A., Frank, R.N., and Varma, S.D. Galactitol accumulation by glucose-6-phosphate deficient fibroblasts: A cellular model for resistance to the complications of diabetes mellitus. Life Sci. 33:1277-1283, 1983. * Laconi, E., Dessi, S., Batetta, B., Pani, P., Pirisi, L., Andria, C., and Macciotta, A. Effect of phenobarbital treatment on erythrocyte glucose-6-phosphate dehydrognenase in human newborns. Pediatr.Pharmacol. 3:59-62, 1983.

* Matsuura, R., Kishi, T., Okahata, H., Kobayashi, M., Tanabe, A., Sakura, N., Sawano, K., and Usui, T. Functional analysis of polymorphonuclear leukocytes in siblings of glucose-6-phosphate dehydrogenase deficiency. Hiroshima J.Med.Sci. 32:173-178, 1983. * Meloni, T., Forteleoni, G., Dore, A., and Cutillo, S. Neonatal hyperbilirubinemia in heterozygous glucose-6-phosphate dehydrogenase deficient females. Br.J.Haematol. 53:241-246, 1983. * Miguel, A., Ramon, M., Petitpierre, E., Goos, A.A., Vermeesch-Markslag, A.M.G., and Vermorken, A.J.M. Population screening for glucose-6-phosphate dehydrogenase deficiency on the Baleares. Hum.Genet. 64:176-179, 1983. * Morisaki, T., Fujii, H., Takegawa, S., Tani, K., Hirono, A., Takizawa, T., Takahashi, K., Shinogi, M., Teshirogi, T., and Miwa, S. G6PD Sendagi: A new glucose-6-phosphate dehydrogenase variant associated with congenital hemolytic anemia. Hum.Genet. 65:214-215, 1983. * Perona, G., Guidi, G.C., Tummarello, D., Mareni, C., Battistuzzi, G., and Luzzato, L. A new glucose-6-phosphate dehydrogenase variant (G-6-PD Verona) in a patient with myelodysplastic syndrome. Scand.J.Haematol. 30:407-414, 1983. * Pootrakul, P. and Panich, V. Effect of acetaminophen on glucose-6-phosphate dehydrogenase, Mahidol variant. Acta Haematol.(Basel) 69:358-359, 1983. * Roth, E.F.,Jr., Raventos-Suarez, C., Rinaldi, A., and Nagel, R.L. Glucose-6-phosphate dehydrogenase deficiency inhibits in vitro growth of Plasmodium falciparum. Proc.Natl.Acad.Sci.USA 80:298-299, 1983. * Saha, N., Samuel, A.P.W., Omer, A., and Hoffbrand, A.V. The inter- and intra-tribal distribution of red cell G6PD phenotypes in Sudan. Hum.Hered. 33:39-43, 1983. * Saha, N., Elamin, F.M., and Samuel, A.P.W. Electrophoretic and quantitative studies of red cell glucose-6-phosphate dehydrogenase in the one-humped camel in the Sudan. Comp.Biochem.Physiol. 75B:189-194, 1983. * Tishler, M. Phenazopyridine-induced hemolytic anemia in a patient with G-6-PD deficiency. Acta Haematol.(Basel) 70:208-209, 1983. Notes: A provocative trial was done giving the patient 400 mg of phenazopyridine in four divided doses. 2 days later the Hb fell to 7.7 g/dl with a Hct. of 0.24. * Travis, S.E. and O'Neal, P.L. Measurement of red cell enzymes in newborn infants. Ann.Clin.Lab.Sci. 13:67-75, 1983. * van Noorden, C.J.F., Tas, J., and Vogels, I.M.C. Cytophotometry of glucose-6-phosphate dehydrogenase activity in individual cells. Histochem.J. 15:583-599, 1983. * Walker, D.H., Hawkins, H.K., and Hudson, P. Fulminant Rocky Mountain spotted fever. Arch.Pathol.Lab.Med. 107:121-125, 1983. * Yoshida, A. and Beutler, E. G-6-PD Variants: Another up-date. Ann.Hum.Genet. 47:25-38, 1983. Notes: (B625). * Allahyari, R., Strother, A., Fraser, I.M., and Verbiscar, A.J. Synthesis of certain hydroxy analogues of the antimalarial drug primaquine and their in vitro methemoglobin-producing and glutathione-depleting activity in human erythrocytes. J.Med.Chem.. 27:407-10, 1984. * Ashmun, R.A., Hultquist, D.E., and Schultz, J.S. Quantitation of glucose-6-phosphate dehydrogenase in single cells by microspectrophotometry. In: The Red Cell: Sixth Ann Arbor Conference,Anonymous New York:Alan R. Liss, Inc. 1984,p. 309-322.

* Beutler, E. Clonal remission in acute leukemia. N.Engl.J.Med. 311:922-923, 1984. Notes: (B690). * Beutler, E. Glucose-6-phosphate dehydrogenase deficiency in drug-induced hemolysis. In: Current Therapy in Internal Medicine, edited by Bayless, T.M., Brain, M.C., and Cherniak, R.M.St. Louis:C. V. Mosby Co. 1984,p. 279-281. Notes: (B686). * Beutler, E. and Bedros, A.A. Unpublished , 1984. Notes: g 6 pd Riverside-- patient=Seth Nichols and Loma Linda--Patient Jimmy Pena. * Beutler, E. Sensitivity to drug-induced hemolytic anemia in glucose-6-phosphate dehydrogenase deficiency. Banbury Rep. 16:205-211, 1984. Notes: (B685). * Beutler, E. Multicentric origin of colon carcinoma. Science 224:630, 1984. Notes: (B681). * Beutler, E. and Maurer, H.S. Unpublished , 1984. Notes: g 6 pd Great Lakes (pt. William Cornwall). * Beutler, E. Acetaminophen and G-6-PD deficiency. Acta Haematol.(Basel) 72:211-212, 1984. Notes: (B692). * Bhattacharya, J. and Mitra, S.S. Mediterranean type of G-6-PD deficiency in Bengalees. Ind.J.Haematol. 2:19-21, 1984. * Chan, C.K. Measurement of erythrocyte glucose-6-phosphate dehydrogenase activity using a centrifugal analyzer. Med.Lab.Sci. 41:112-120, 1984. * Charles, D.J. and Pretsch, W. A mouse mutant deficient in erythrocyte glucose-6-phosphate dehydrogenase after paternal ethylnitrosourea treatment. Genetics 107:S19, 1984. * Cin, S., Akar, N., Arcasoy, A., Dedeoglu, S., and Cavdar, A.O. Prevalence of thalassemia and G-6-PD deficiency in North Cyprus. Acta Haematol.(Basel) 71:69-70, 1984. * Descalzi-Cancedda, F., Caruso, C., Romano, M., Di Prisco, G., and Camardella, L. Amino acid sequence of the carboxy-terminal end of human erythrocyte glucose-6-phosphate dehydrogenase. Biochem.Biophys.Res.Commun. 118:332-338, 1984. * Du, C.S., Xu, Y.K., Wu, Q.L., Liu, L.B., and Wu, M. Studies on erythrocyte glucose-6-phosphate dehydrogenase variants in Chinese. III. Gd(-) Miaozu-Baisha. Acta Genet.Sinica 11:153-158, 1984. * El-Hazmi, M.A.F. and Warsy, A.S. Aspects of sickle cell gene in Saudi Arabia - interaction with glucose-6-phosphate dehydrogenase deficiency. Hum.Genet. 68:320-323, 1984. * Entan, P. Glucose-6-phosphate dehydrogenase deficiency in Sichuan. Unpublished , 1984. * Farmer, E.E. and Easterby, J.S. The purification of yeast glucose 6-phosphate dehydrogenase by dye-ligand chromatagraphy. Anal.Biochem. 141:79-82, 1984. * Ferraris, A.M., Broccia, G., Meloni, T., Canepa, L., Sessarego, M., and Gaetani, G.F. Clonal origin of cells restricted to monocytic differentiation in acute nonlymphocytic leukemia. Blood 64:817-820, 1984. * Fujii, H., Miwa, S., Takegawa, S., Takahashi, K., Hirono, A., Takizawa, T., Morisaki, T., Kanno, H., Taguchi, T., and Okamura, J. Gd(-) Gifu and Gd(-) Fukuoka. Two new variants of glucose-6-phosphate dehydrogenase found in Japan. Hum.Genet. 66:276-278, 1984. * Grimmond, T.R. and Cameron, A.S. Primaquine-chloroquine

prophylaxis against malaria in Southeast-Asian refugees entering South Australia. Med.J.Aust. 140:322-5, 1984. * Howard-Peebles, P.N. and Carroll, A.J. Recombination between the Fragile X and G6PD. Am.J.Med.Genet. 17:275-276, 1984. * Ishwad, C.S. and Naik, S.N. A new glucose-6-phosphate dehydrogenase variant (G-6-PD Kalyan) found in a Koli family. Hum.Genet. 66:171-175, 1984. Notes: G-6-PD Kalyan. * Jacobson, R.J., Temple, M.J., Singer, J.W., Raskind, W., Powell, J., and Fialkow, P.J. A clonal complete remission in a ptatient with acute nonlymphocytic leukemia originating in a multipotent stem cell. N.Engl.J.Med. 310:1513-1517, 1984. * Kano, M. and Opolsky, A.F. Distribution and frequency of glucose-6-phosphate deficiency in the central region of Cuba. Genetika 20:864-867, 1984. * Lachant, N., Tomoda, A., and Tanaka, K.R. Inhibition of the pentose phosphate shunt by lead: A potential mechanism for hemolysis in lead poisoning. Blood 63:518-524, 1984. * Lubbers, J.R., Chauhan, S., Miller, J.K., and Bianchine, J.R. The effects of chronic administration of chlorite to glucose-6-phosphate dehydrogenase deficient healthy adult male volunteers. J.Environ.Pathol.Toxicol.Oncol. 5:239-242, 1984. Notes: Under controlled laboratory conditions, the safety of daily ingestion of 5 ppm chlorine dioxide, chlorite and chlorate by normal healthy adult males has been established. To determine the effect upon potentially susceptible individuals, a parallel chronic human investigation was undertaken. Study subjects were three healthy adult males deficient in glucose-6-phosphate dehydrogenase. These volunteers received 500 ml of sodium chlorite at a concentration of 5 ppm daily for twelve consecutive weeks; the subsequent observation period extended an additional eight weeks. Upon evaluation of an extensive battery of tests designed to measure the biochemical and physiological response to chlorite ingestion, no clinically significant changes were detected. AD - Department of Pharmacology AD - Ohio State University AD - College of Medicine, Columbus. * Mohandas, T., Sparkes, R.S., Bishop, D.F., Desnick, R.J., and Shapiro, L.J. Frequency of reactivation and variability in expression of X-linked enzyme loci. Am.J.Hum.Genet. 36:916-925, 1984. * Morelli, A., Benatti, U., Guida, L., and De Flora, A. G-6-PD Cagliari: A new low activity glucose-6-phosphate dehydrogenase variant characterized by enhanced intracellular lability. Hum.Genet. 66:62-65, 1984. * Morelli, A., Benatti, U., Guida, L., and De Flora, A. Mediterranean glucose-6-phosphate dehydrogenase (G6PD) deficiency -- Near normal decay of the mutant enzyme protein in circulating erythrocytes. Scand.J.Haematol. 33:144-154, 1984. * Niehaus, W.G.,Jr. and Dilts, R.P.,Jr. Purification and characterization of glucose-6-phosphate dehydrogenase from Aspergillus parasiticus. Arch.Biochem.Biophys. 228:113-119, 1984. Notes: Glucose-6-phosphate dehydrogenase (EC 1.1.1.49) was purified from mycelium of Aspergillus parasiticus (1-11-105 Whl). The enzyme had a molecular weight of 1.8 X 10(5) and was composed of four subunits of apparently equal size. The substrate was very strict, only glucose 6- phosphate and glucose being oxidized by NADP or thio-NADP. Zinc ion was a powerful inhibitor of the enzyme, inhibition being competitive with respect to glucose 6-phosphate, with Ki about 2.5 microM. Other divalent metal ions which also serve as inhibitors are nickel, cadmium, and cobalt.

It is proposed that the stimulation of polyketide synthesis by zinc ion may be mediated in part by inhibition. of glucose-6-phosphate dehydrogenase. * Prchal, J., Garner, C., and Tomana, M. Sugar alditols in normal and G-6-PD deficient (A-) erythrocytes. Clin.Res. 32:498A, 1984. * Roos, D. and Verweij, S.L. Oorspronkelijke stukken. Genessmiddelen en andere stoffen die bij personen met glucose-6-fosfaat-dehydrogenase-defici ntie kunnen leiden tot versterkte hemolyse. Ned.Tijdschr.Geneeskd. 128:244-245, 1984. * Roos, D. and Verweij, S.L. Drugs and other agents leading to increased hemolysis in persons with glucose-6-phosphate dehydrogenase deficiency. Ned.Tijdschr.Geneeskd. 128:244-5, 1984. * Saenz, G.F., Chaves, M., Berrantes, A., Elizondo, J., Montero, A.G., and Yoshida, A. A glucose-6-phosphate dehydrogenase variant, Gd(-) Santamaria found in Costa Rica. Acta Haematol.(Basel) 72:37-40, 1984. * Sansone, G., Reali, S., Sansone, R., and Allegranza, F. Acute hemolytic anemia induced by a pyrazolonic drug in a child with glucose-6-phosphate dehydrogenase deficiency. Acta Haematol.(Basel) 72:285-287, 1984. * Schroeder, L., Christoff, M., and Levy, H.R. Glucose-6-phosphate dehydrogenase from rabbit erythrocytes. Biochim.Biophys.Acta 784:48-52, 1984. * Shalev, O., Wollner, A., and Menczel, J. Diabetic ketoacidosis does not precipitate haemolysis in patients with the Mediterranean variant of glucose-6-phosphate dehydrogenase deficiency. BMJ 288:179-180, 1984. * Solem, E. Glucose-6-phosphate dehydrogenase deficiency: An easy and sensitive quantitative assay for the detection of female heterozygotes in red blood cells. Clin.Chim.Acta 142:153-160, 1984. * Takizawa, T., Fujii, H., Takagawa, S., Hirono, A., Morisaki, T., Kanno, H., Oka, R., Yoshioka, H., Miwa, S., and Takahashi, K. A unique electrophoretic slow-moving glucose 6-phosphate dehydrogenase variant (G6PD Asahikawa) with a markedly acidic pH optimum. Hum.Genet. 68:70-72, 1984. * Tanaka, K.R., Beutler, E., Kaplow, L.S., Plapinger, R.E., and Yoshida, A. Screening red blood cell glucose-6-phosphate dehydrogenase activity. NCCLS 4:360-366, 1984. Notes: (B694). * Toncheva, D. and Tzoneva, M. Genetic polymorphism of G6PD in a Bulgarian population. Hum.Genet. 67:340-342, 1984. * Toniolo, D., Persico, M.G., Battistuzzi, G., and Luzzatto, L. Partial purification and characterization of the messenger RNA for human glucose-6-phosphate dehydrogenase. Mol.Biol.Med. 2:89-103, 1984. * Tzoneva, M., Mavrudieva, M., Toncheva, D., and Lalchev, S. Glucose-6-phosphate dehydrogenase deficiency and Rh factor. Haematologia (Budap) 17:399-403, 1984. * Ventura, A., Panizon, F., Soranzo, M.R., Veneziano, G., Sansone, G., Testa, U., and Luzzatto, L. Congenital dyserythropoietic anaemia type II associated with a new type of G6PD deficiency (G6PD Gabrovizza). Acta Haematol.(Basel) 71:227-234, 1984. Notes: A 6-year-old boy with chronic haemolytic anaemia was found to have glucose 6-phosphate dehydrogenase (G6PD) deficiency and the morphological, ultrastructural and serological features of congenital dyserythropoietic anaemia (CDA) type II. The patient's mother was heterozygous for G6PD deficiency. G6PD from the

patient's red cells, upon partial purification and full characterization, was found to be a new variant designated G6PD Gabrovizza. We conclude that two distinct genetic abnormalities coexisted in this patient. We suggest that CDA type II may become clinically more expressed when another abnormality of the erythrocytes coexists. * Weimer, T.A., Schueler, L., Beutler, E., and Salzano, F.M. Gd (+) Laguna, a new rare glucose-6-phosphate dehydrogenase variant from Brazil. Hum.Genet. 65:402-404, 1984. Notes: (B645). * Yeh, G.C., Roth, E.F.,Jr., Phang, J.M., Harris, S.C., Nagel, R.L., and Rinaldi, A. The effect of pyrroline-5-carboxylic acid on nucleotide metabolism in erythrocytes from normal and glucose-6-phosphate dehydrogenase-deficient subjects. J.Biol.Chem. 259:5454-5458, 1984. * Anonymous Glucose-6-phosphate dehydrogenase deficiency. Report of a WHO working group. WHO Geneva,3-4 September, 1985. * Abkowitz, J.L., Ott, R.L., Nakamura, J.M., Steinmann, L., Fialkow, P.J., and Adamson, J.W. Feline glucose-6-phosphate dehydrogenase cellular mosaicism. J.Clin.Invest. 75:133-140, 1985. * Barretto, O.C.O., Cardoso, and De Cillo, D. Viscerocutaneous form of loxoscelism and erythrocyte glucose-6-phosphate deficiency. Rev.Inst.Med.trop Sao Paulo 27:264-267, 1985. * Battistuzzi, G., D'Urso, M., Toniolo, D., Persico, G.M., and Luzzatto, L. Tissue-specific levels of human glucose-6-phosphate dehydrogenase correlate with methylation of specific sites at the 3' end of the gene. Proc.Natl.Acad.Sci.USA 82:1465-1469, 1985. * Bernstein, R.E. Glycosylated haemoglobin in glucose-6-phosphate dehydrogenase deficiency. Lancet 2:332-333, 1985. * Beutler, E., Davis, S., Forman, L., and Gelbart, T. Unpublished , 1985. Notes: G 6 PD Pompton Plains. Patient-- Robert Glazier. * Beutler, E. G-6-PD deficiency. JAMA 254:1234, 1985. Notes: (B709). * Beutler, E., Forman, L., and Gelbart, T. Unpublished , 1985. Notes: G 6 PD Indianapolis. Patient-- Leonard Sanquennetti. Physician-- Dr. Oei. * Beutler, E., Kuhl, W., and Gelbart, T. 6-Phosphogluconolactonase deficiency, a hereditary erythrocyte enzyme deficiency: Possible interaction with glucose-6-phosphate dehydrogenase deficiency. Proc.Natl.Acad.Sci.USA 82:3876-3878, 1985. Notes: (B705). * Clemens, M.R., Einsele, H., and Waller, H.D. The fatty acid composition of red cells deficient in glucose-6-phosphate dehydrogenase and their susceptibility to lipid peroxidation. Klin.Wochenschr. 63:578-582, 1985. * Colonna-Romano, S., Iolascon, A., Lippo, S., Pinto, L., Cutillo, S., and Battistuzzi, G. Genetic heterogeneity at the glucose-6-phosphate dehydrogenase locus in southern Italy: A study on the population of Naples. Hum.Genet. 69:228-232, 1985. * De Flora, A. The technology of carrier erythrocytes: A versatile tool for diagnosis and therapy. In: Biotechnology in Diagnostics, edited by Koprowski, H., Ferrone, S., and Albertini, A.New York:Elsevier/North-Holland, 1985,p. 223-236.

* Der Kaloustian, V.M. G6PD deficiency and neonatal jaundice. Unpublished , 1985. * Du, C.S., Hua, X.Y., Wu, Q.L., Li, C.Q., Zhen, J.F., and Li, H.L. Studies on erythrocyte glucose-6-phosphate dehydrogenase variants in Chinese. IV. Gd(-) Gaohe associated with paroxysmal nocturnal hemoglobinuria. Chinese J.Pathophysiol. 1:12-15, 1985. * Haghighi, B., Suzangar, M., Yazdani, A., and Mehnat, M. A genetic variant of human erythrocyte glucose 6-phosphate dehydrogenase. Biochem.Biophys.Res.Commun. 132:1151-1159, 1985. * Halliwell, B. Effect of oxidized glutathione on the inhibition of glucose-6-phosphate dehydrogenase by NADPH. Biochem.J. 234:741, 1985. * Jansen, G., Koenderman, L., Rijksen, G., Cats, P.B., and Staal, G.E.J. Characteristics of hexokinase, pyruvate kinase, and glucose-6-phosphate dehydrogenase during adult and neonatal reticulocyte maturation. Am.J.Hematol. 20:203-215, 1985. * Jansen, G., Koenderman, L., Rijksen, G., Punt, K., Dekker, A.W., and Staal, G.E.J. Age dependent behaviour of red cell glycolytic enzymes in haematological disorders. Br.J.Haematol. 61:51-59, 1985. * Jeffery, J., Hobbs, L., and Jrnvall, H. Glucose-6-phosphate dehydrogenase from Saccharomyces cerevisiae: Characterization of a reactive lysine residue labeled with acetylsalicylic acid. Biochemistry 24:666-671, 1985. * Kageoka, T., Satoh, C., Goriki, K., Fujita, M., Neriishi, S., Yamamura, K., Kaneko, J., and Masunari, N. Electrophoretic variants of blood proteins in Japanese IV. Prevalence and enzymological characteristics of G6PD variants in Hiroshima and Nagasaki. Hum.Genet. 70:101-108, 1985. * Karadsheh, N.S. Pyruvate kinase and glucose-6-phosphate dehydrogenase deficiencies in Jordan. Dirasat 12:75-80, 1985. * Lachant, N.A., Gottlieb, A.J., DiFino, S.M., Landaw, S.A., and Tanaka, K.R. Increased Heinz body formation and impaired erythrocyte pentose phosphate shunt function during pregnancy. Am.J.Hematol. 18:131-141, 1985. * Lisker, R., Perez-Briceno, R., and Beutler, E. A new glucose-6-phosphate dehydrogenase variant, Gd(-) Tepic, characterized by moderate enzyme deficiency and mild episodes of hemolytic anemia. Hum.Genet. 69:19-21, 1985. Notes: (B707). * Luzzatto, L. and Battistuzzi, G. Glucose-6-phosphate dehydrogenase. In: Advances in Human Genetics, edited by Harris, H. and Hirschhorn, K.New York:Plenum Press, Inc. 1985,p. 217-329. * Mamlok, R.J., Mills, G.C., Goldblum, R.M., and Daeschner, C.W.I. Glucose-6-phosphate dehydrogenase Beaumont: A new variant with severe enzyme deficiency and chronic nonspherocytic hemolytic anemia. Enzyme 34:15-21, 1985. * Martin-DeLeon, P.A., Wolf, S.F., Persico, G., Toniolo, D., Martini, G., and Migeon, B.R. Localization of glucose-6-phosphate dehydrogenase in mouse and man by in situ hybridization: Evidence for a single locus and transposition of homologous X-linked genes. Cytogenet.Cell Genet. 39:87-92, 1985. * Migeon, B.R., Wolf, S.F., Axelman, J., Kaslow, D.C., and Schmidt, M. Incomplete X chromosome dosage compensation in chorionic villi of human placenta. Proc.Natl.Acad.Sci.USA 82:3390-3394, 1985. * Nour-Eldeen, A.F., Craig, M.M., and Gresser, M.J. Interaction of inorganic vanadate with glucose-6-phosphate dehydrogenase. J.Biol.Chem. 260:6836-6842, 1985. * Prchal, J.T., Harmon, W.A., and Hall, K.B. Gilbert's

syndrome associated with new variant of G6PD deficiency: G6PD-Pawnee. Unpublished , 1985. * Rosenbloom, B.E., Rosenfelt, F.P., Ullman, H., and Weinstein, I.M. Cytomegalovirus infection and hemolytic anemia due to glucose-6-phosphate dehydrogenase deficiency. Mt.Sinai J.Med. 52:363-366, 1985. * Shalev, O., Lavi, V., Hebbel, R.P., and Eaton, J.W. Erythrocyte (Ca+2 and Mg+2)-ATPase activity: Increased sensitivity to oxidative stress in glucose-6-phosphate dehydrogenase deficiency. Am.J.Hematol. 19:131-136, 1985. * Shalev, O., Eliakim, R., Lugassy, G.Z., and Menczel, J. Hypoglycemia-induced hemolysis in glucose-6-phosphate dehydrogenase deficiency. Acta Haematol.(Basel) 74:227-229, 1985. * Usanga, E.A. and Luzzatto, L. Adaptation of plasmodium falciparum to glucose 6-phosphate dehydrogenase-deficient host red cells by production of parasite-encoded enzyme. Nature 313:793-795, 1985. * Vaca, G., Ibarra, B., Garcia-Cruz, D., Medina, C., Romero, F., Cantu, J.M., and Beutler, E. G-6-PD Jalisco and G-6-PD Morelia: Two new Mexican variants. Hum.Genet. 71:82-85, 1985. Notes: (B710) Jalisco patient--Mario Martinez. Morelia patient--Juan Maldonado. * Valentine, W.N., Tanaka, K.R., and Paglia, D.E. Hemolytic anemias and erythrocyte enzymopathies. Ann.Intern.Med. 103:245-257, 1985. * van Noorden, C.J.F. and Vogels, I.M.C. A sensitive cytochemical staining method for glucose-6-phosphate dehydrogenase activity in individual erythrocytes. Br.J.Haematol. 60:57-63, 1985. * Vergnes, H.A., Bonnet, L.G., and Grozdea, J.D. Genetic variants of human erythrocyte glucose-6-phosphate dehydrogenase: New characterization data obtained by multivariate analysis. Ann.Hum.Genet. 49:1-9, 1985. * Veronesi, F.M., Stangoni, A., Cuccuru, G.B., Mulas, G., Marogna, G., Cossu, G., and Pettener, D. Glucose-6-phosphate dehydrogenase deficiency and blood groups in Northern Sardinia. Hum.Hered. 35:399-402, 1985. * Veronesi, M.F., Stagoni, A., Cuccuru, G.B., Mulas, G., Marogna, G., Cossu, G., and Pettener, D. Glucose-6-phosphate dehydrogenase deficiency and blood groups in northern Sardinia. Hum.Hered. 35:399, 1985. * Warsy, A.S. Frequency of glucose-6-phosphate dehydrogenase deficiency in sickle-cell disease. Hum.Hered. 35:143-147, 1985. * Xu, Y. Investigation of RBC-G6PD deficiency gene frequency in 9 nationality populations in 7 provinces (autonomous region) of China. Heredity and Disease 2:67-71, 1985. * Anonymous Glucose-6-Phosphate Dehydrogenase, Orlando, FL:Academic Press, Inc. 1986. Notes: (B792). * Amoruso, M.A., Ryer, J., Easton, D., Witz, G., and Goldstein, B.D. Estimation of risk of glucose 6-phosphate dehydrogenase-deficient red cells to ozone and nitrogen dioxide. J.Occup.Med. 28:473-479, 1986. Notes: It has been suggested that the more than 1 million black Americans with the A- variant of glucose-6-phosphate dehydrogenase deficiency (G6PD) are at risk for adverse hematologic effects due to inhalation of ambient levels of oxidant gases. To evaluate this hypothesis studies were performed that included direct exposure of human G6PD-deficient red cells, and of mouse strains with different G6PD levels, to the oxidant

gases ozone and nitrogen dioxide. Using the oxidant drug phenylhydrazine in part as a point of comparison, conservative extrapolation of the data indicates that exposure to levels of ozone or nitrogen dioxide at least one and probably two orders of magnitude above the LD50 would be required for any hematologic effect to be observed of pertinence to G6PD deficiency. It is concluded that there is no reason to remove or preclude from the workplace black employees with the common A- variant of red cell G6PD deficiency who potentially are exposed to oxidant gases. * Ashmun, R.A., Hultquist, D.E., and Schultz, J.S. Kinetic analysis in single, intact cells by microspectrophotometry: evidence for two populations of erythrocytes in an individual heterozygous for glucosse-6-phosphate dehydrogenase deficiency. Am.J.Hematol. 23:311-316, 1986. * Avissar, N., Farkash, Y., and Shaklai, M. Erythrocyte enzymes in polycythemia vera: A comparison to erythrocyte enzyme activities of patients with iron deficiency anemia. Acta Haematol.(Basel) 76:37-43, 1986. * Baird, J.K., Davidson, D.E.,Jr., and Decker-Jackson, J.E. Oxidative activity of hydroxylated primaquine analogs. Non-toxicity to glucose-6-phosphate dehydrogenase-deficient human red blood cells in vitro. Biochem.Pharmacol. 35:1091-1098, 1986. * Beutler, E., Forman, L., and del Alarcon, P.A. Unpublished , 1986. Notes: G 6 PD Iowa and Iowa City. Iowa City characterized from Dale Hornberg, uncle of patient Jeffrey Kirchner. Iowa characterized from Ray Barlow, uncle of patient Jeremy Oliver. Both variants are Mg-NADP reactivated. * Beutler, E. and Kuhl, W. Characteristics and significance of the reverse glucose-6-phosphate dehydrogenase reaction. J.Lab.Clin.Med. 107:502-507, 1986. Notes: (B734). * Beutler, E. G-6-PD as a marker for tumors. In: Glucose-6-Phosphate Dehydrogenase, edited by Yoshida, A. and Beutler, E.Orlando, FL:Academic Press, Inc. 1986,p. 455-462. Notes: (B743). * Beutler, E., Hartman, K., Gelbart, T., and Forman, L. G-6-PD Walter Reed: Possible insight into "structural" NADP in G-6-PD. Am.J.Hematol. 23:25-30, 1986. Notes: (B736). * Beutler, E. X-inactivation in heterozygous G-6-PD variant females. In: Glucose-6-Phosphate Dehydrogenase, edited by Yoshida, A. and Beutler, E.Orlando, FL:Academic Press, Inc. 1986,p. 405-415. Notes: (B741). * Beutler, E. Drug induced hemolytic anemia and non-spherocytic hemolytic anemia. In: Glucose-6-Phosphate Dehydrogenase, edited by Yoshida, A. and Beutler, E.Orlando, FL:Academic Press, Inc. 1986,p. 3-12. Notes: (B742). * Bowen, D.A., Foadi, M.D., and Owen, J. Fatal familial haemolytic anaemia. Am.J.Forensic.Med.Pathol. 7:62-63, 1986. Notes: A 19-year-old man, mentally handicapped but physically well, died within 2 days of onset of an acute episode of gastrointestinal upset and "haematuria." Autopsy and microscopy suggested a haemolytic episode and family studies showed haemolytic anemia due to glucose-6- phosphate dehydrogenase deficiency, which was almost certainly present in the deceased. * Buckwitz, D., Schoenian, G., Holzhuetter, H.G., and Jacobasch, G. Kinetic model of glucose-6-phosphate dehydrogenase

from red blood cells. Parameter estimation from progress curves and simulation of regulatory properties. Biomed.Biochim.Acta 45:429-439, 1986. * Corrons, J.L.V., Merino, A., and Pujades, M.A. A sensitive cytochemical staining method for glucose-6-phosphate dehydrogenase (G6PD) activity in individual erythrocytes. Br.J.Haematol. 63:400-402, 1986. * Dovrat, A., Scharf, J., Eisenbach, L., and Gershon, D. G6PD moleculares devoid of catalytic activity are present in the nucleus of the rat lens. Exp.Eye Res. 42:489-496, 1986. * El-Hazmi, M.A.F., Al-Swailem, A.R., Al-Faleh, F.Z., and Warsy, A.S. Frequency of glucose-6-phosphate dehydrogenase, pyruvate kinase and hexokinase deficiency in the Saudi population. Hum.Hered. 36:45-49, 1986. * El-Hazmi, M.A.F. and Warsy, A.S. Glucose-6-phosphate dehydrogenase polymorphism in the Saudi population. Hum.Hered. 36:24-30, 1986. * Fok, T. and Lau, S. Glucose-6-phosphate dehydrogenase deficiency: A preventable cause of mental retardation. BMJ 292:829, 1986. * Hafez, M., Amar, E.S., Zedan, M., Hammad, H., Sorour, A.H., El-Desouky, E.S., and Gamil, N. Improved erythrocyte survival with combined vitamin E and selenium therapy in children with glucose-6-phosphate dehydrogenase deficiency and mild chronic hemolysis. J.Pediatr. 108:558-561, 1986. Notes: To study the antioxidant effect of high-dose vitamin E alone and in combination with selenium in patients with glucose-6-phosphate dehydrogenase deficiency with mild chronic hemolysis, 36 male children with such manifestations were enrolled consecutively into two equal groups. Group 1 received 800 IU vitamin E daily, and group 2 received 800 IU vitamin E in combination with 25 micrograms selenium. Hematologic status before and 2 months after treatment was evaluated. After treatment there was a significant change toward normal in both groups. The mean red cell half-life increased in group 1 from 16.9 to 22.8 days (P less than 0.01), and in group 2 from 15.6 to 24.3 days (P less than 0.01). A comparison of the mean difference of paired values in the two groups revealed a more significant increase in hemoglobin (0.9 +/- 0.1 gm/dl vs 1.2 +/0.2 gm/dl, P less than 0.05), hematocrit (2.4% +/- 0.4% vs 3.8% +/- 0.3%, P less than 0.05), and red cell half-life (5.9 +/- 3.0 days vs 9.1 +/- 4.4 days, P less th * Horton, H.M. and Calabrese, E.J. Predictive models for human glucose-6-phosphate dehydrogenase deficiency. Drug Metab.Rev. 17:261-281, 1986. * Jackson, L.C., Chandler, J.P., and Jackson, R.T. Inhibition and adaptation of red cell glucose-6-phosphate dehydrogenase (G6PD) in vivo to chronic sublethal dietary cyanide in an animal model. Hum.Biol. 58:67-78, 1986. * Janney, S.K., Joist, J.H., and Fitch, C.D. Excess release of ferriheme in G6PD erythrocytes: Possible cause of hemolysis and resistance to malaria. Blood 67:331-333, 1986. * Jansen, G., Hepkema, B.G., van der Vegt, S.G.L., and Staal, G.E.J. Glycolytic activity in human red cell populations separated by a combination of density and counterflow centrifugation. Evidence for an improved separation of red cells according to age. Scand.J.Haematol. 37:189-195, 1986. * Karadsheh, N.S., Awidi, A.S., and Tarawneh, M.S. Two new glucose-6-phosphate dehydrogenase (G6PD) variants associated with hemolytic anemia: G6PD Amman-1 and G6PD Amman-2. Am.J.Hematol.

22:185-192, 1986. * Kasper, M.L., Miller, W.J., and Jacob, H.S. G6PD-deficiency infectious haemolysis: a complement dependent innocent bystander phenomenon. Br.J.Haematol. 63:85-91, 1986. * Khan, P.M., Ploem, J.E., Wijnen, J.T., Breukel, C., Korthof, G., and Weening, R.S. G6PD Volendam: De Novo mutation of unusual mechanism in a severly deficient Dutch female born to apparently normal parents. 7th International Congress of Human Genetics:418a, 1986. * Khan, P.M., Ploem, J.E., Wijnen, J.T., Breukel, C., Korthof, G., and Weening, R.S. De novo mutation at G6PD locus with clinical consequences in a Dutch female. Am.J.Hum.Genet. 39(Suppl):A14, 1986. * Kirkman, H.N. and Gaetani, G.F. Regulation of glucose-6-phosphate dehydrogenase in human erythrocytes. J.Biol.Chem. 261:4032-4038, 1986. * Kirkman, H.N., Gaetani, G.F., and Clemons, E.H. NADP-binding proteins causing reduced availability and sigmoid release of NADP+ in human erythrocytes. J.Biol.Chem. 261:4039, 1986. * Luzzatto, L., O'Brien, S., Usanga, E., and Wanachiwanawin, W. Origin of G6PD polymorphism: Malaria and G6PD deficiency. In: Glucose-6-Phosphate Dehydrogenase, edited by Yoshida, A. and Beutler, E.Orlando,FL:Academic Press, Inc. 1986,p. 181-193. * Luzzatto, L. Glucose-6-phosphate dehydrogenase and other genetic factors interacting with drugs. Prog.Clin.Biol.Res. 214:385-399, 1986. * Luzzatto, L. Glucose-6-phosphate dehydrogenase and other genetic factors interacting with drugs. In: Ethnic Differences in Reactions to Drugs and Xenobiotics,Anonymous 1986,p. 385-399. * Magnani, M., Stocchi, V., Canestrari, F., Cucchiarini, L., Stocchi, O., Coppa, G.V., Felici, L., Giorgi, P.L., and Fornaini, G. Redox and energetic state of red blood cells in G6PD deficiency, hererozygous beta-thalassemia and the combination of both. Acta Haematol.(Basel) 75:211-214, 1986. * Martini, G., Toniolo, D., Vulliamy, T., Luzzatto, L., Dono, R., Viglietto, G., Paonessa, G., D'Urso, M., and Persico, M.G. Structural analysis of the X-linked gene encoding human glucose 6-phosphate dehydrogenase. EMBO J. 5:1849-1855, 1986. * Martini, G., Vulliamy, T., and Luzzatto, L. Unpublished , 1986. * Mimouni, F., Shohat, S., and Reisner, S.H. G6PD-deficiency donor blood as a cause of hemolysis in two preterm infants. Isr.J.Med.Sci. 22:120-122, 1986. * Monzon, C.M., Fairbanks, V.F., Burgert, E.O.,Jr., Sutherland, J.E., and Elliot, S.C. Hereditary red cell disorders in Southeast Asian refugees and the effect on the prevalence of thalassemia disorders in the United States. Am.J.Med.Sci. 29:147-151, 1986. * Nieuwenhuis, F., Wolf, B., Bomba, A., and De Graaf, P. Haematological study in Cabo Delgado province, Mozambique; sickle cell trait and G6PD deficiency. Trop.Geogr.Med. 38:183-187, 1986. Notes: A haematological study was done in several villages in the northern province of Cabo Delgado in Mozambique. The prevalence of sickle cell trait (HbAS) was found to be about 4%. The prevalence of G6PD deficiency in males was about 18%. No significant differences were found in haemoglobin values between HbAA and HbAS individuals and between G6PD deficient and G6PD normal individuals. The number of males with both HbAS and G6PD deficiency was not significantly greater than expected.

* Omenn, G.S. Susceptibility to occupational and environmental exposures to chemicals. Prog.Clin.Biol.Res. 214:527-545, 1986. * Panich, V. G6PD variants in southern Asian populations. In: Glucose-6-Phosphate Dehydrogenase, edited by Yoshida, A. and Beutler, E.Orlando, FL:Academic Press, Inc. 1986,p. 195-241. Notes: (B741). * Persico, M.G., Viglietto, G., Martini, G., Dono, R., D'Urso, M., Toniolo, D., Vulliamy, T., and Luzzatto, L. Analysis of the primary structure of human G 6 PD deduced from the cDNA sequence. In: Glucose-6-Phosphate Dehydrogenase, edited by Yoshida, A. and Beutler, E.Orlando, FL:Academic Press, Inc. 1986,p. 503-516. * Persico, M.G., Viglietto, G., Martino, G., Toniolo, D., Paonessa, G., Moscatelli, C., Dono, R., Vulliamy, T., Luzzatto, L., and D'Urso, M. Isolation of human glucose-6-phosphate dehydrogenase (G6PD) cDNA clones: Primary structure of the protein and unusual 5' non-coding region. Nucleic Acids Res. 14:2511-2522,7822, 1986. * Piomelli, S. G6PD deficiency and hemolytic anemia: G6PD-related neonatal jaundice. In: Glucose-6-Phosphate Dehydrogenase, edited by Yoshida, A. and Beutler, E.Orlando, FL:Academic Press, Inc. 1986,p. 95-108. * Raoult, D., Lena, D., Perrimont, H., Gallais, H., Walker, D.H., and Casanova, P. Haemolysis with Mediterranean spotted fever and glucose-6-phosphate dehydrogenase deficiency. Trans.R.Soc.Trop.Med.Hyg. 80:961-962, 1986. Notes: Mediterranean spotted fever with haemolysis is reported in a glucose- 6-phosphate dehydrogenase deficient Algerian man. The clinical course was unusually severe for a 27-year-old patient. The authors suspect G6PD deficiency to be a cause of enhanced severity in Mediterranean spotted fever as well as in other rickettsioses. * Roth, E.F.,Jr., Ruprecht, R.M., Schulman, S., Vanderberg, J., and Olson, J.A. Ribose metabolism and nucleic acid synthesis in normal and glucose-6-phosphate dehydrogenase-deficient human erythrocytes infected with plasmodium falciparum. J.Clin.Invest. 77:1129-1135, 1986. * Roth, E.F.,Jr., Schulman, S., Vanderberg, J., and Olson, J. Pathways for the reduction of oxidized glutathione in the Plasmodium falciparum-infected erythrocyte: Can parasite enzymes replace host red cell glucose-6-phosphate dehydrogenase? Blood 67:827-830, 1986. * Samuel, A.P. and Saha, N. Distribution of red cell G6PD and 6PGD phenotypes in Saudi Arabia. Trop.Geogr.Med. 38:287-291, 1986. Notes: A total of 1112 randomly selected Saudi Arabs, of both sexes living in Jeddah and the surrounding areas, were studied for the distribution of red cell G6PD and 6PGD phenotypes by the methaemoglobin reduction test and starch-gel electrophoresis. The overall G6PD deficiency was 8.4% in males and 7.0% in females. No deficiency of 6PGD was detected. The gene frequencies at the G6PD locus were as follows: in males [GdB+ - 0.86; GdA+ - 0.05; GdB- - 0.06, GdA- - 0.02] and those in females [GdB+ - 0.85; GdA+ - 0.07; GdB- - 0.06; GdA- - 0.01] respectively. The hyperactive allele, GdBKRT originally detected in the Sudan was also present in a low frequency in Saudi Arabs. The frequency of PGDA and PGDC alleles were found to be 0.94 and 0.06 respectively. There was a significant deviation from the Hardey-Weinberg Equilibrium in the distribution of PGDC alleles with an excess of homozygotes

(chi 2(1): 54.0) and lack of heterozygotes (chi 2(1): 7.31) probably due to the practice of inbreeding for many generations * Samuel, A.P.W., Saha, N., Acquaye, J.K., Omer, A., Ganeshaguru, K., and Hassounh, E. Association of red cell glucose-6-phosphate dehydrogenase with haemoglobinopathies. Hum.Hered. 36:107-112, 1986. Notes: A total of 1,112 randomly selected Saudi Arabs, of both sexes, living in Jeddah and the surrounding areas were screened for the phenotypic distribution of red cell glucose-6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase (6PGD). They were also investigated for haemoglobin and for thalassaemia. Phenotyping of the haemoglobins and the red cell enzymes was carried out by starch gel electrophoresis and the dye-decolouration screening test, while the investigation for thalassaemia was carried out by globin-chain biosynthesis, followed by column chromatography. The red cell Gd- alleles were significantly associated with the sickle-cell gene in both the males (chi 2(1): AS-28.80; SS-4.89) and females (chi 2(1): AS-10.99; SS-13.16). A similar association was also observed between G6PD deficiency and thalassaemias in males (chi 2(1): alpha- thalassaemia - 3.13; beta-thalassaemia - 11.06) and females (chi 2(1): alpha-thalassaemia - 6.63). However, no such association was detected between * Singh, H. Glucose-6-phosphate dehydrogenase deficiency: A preventable cause of mental retardation. BMJ 292:397-398, 1986. * Steinberg, M.H., Gill, F., and Emanuel, B.S. Expression of two G-6-PD genes. Br.J.Haematol. 64:107-110, 1986. * Takizawa, T., Huang, I.Y., Ikuta, T., and Yoshida, A. Human glucose-6-phosphate dehydrogenase: Primary structure and cDNA cloning. Proc.Natl.Acad.Sci.USA 83:4157-4161, 1986. * Toncheva, D. Variants of glucose-6-phosphate dehydrogenase in a Vietnamese population. Hum.Hered. 36:348-351, 1986. * Vogels, I.M.C., van Noorden, C.J.F., Wolf, B.H.M., Saelman, D.E.M., Tromp, A., Schutgens, R.B.H., and Weening, R.S. Cytochemical determination of heterozygous glucose-6-phosphate dehydrogenase deficiency in erythrocytes. Br.J.Haematol. 63:402-405, 1986. * White, J.M., Byrne, M., Richards, R., Buchanan, T., Katsoulis, E., and Weerasingh, K. Red cell genetic abnormalities in peninsular Arabs: sickle haemoglobin, G6PD deficiency, and alpha and beta thalassaemia. J.Med.Genet. 23:245-251, 1986. * Yoshida, A. and Takizawa, T. Molecular cloning of cDNA for G6PD. In: Glucose-6-Phosphate Dehydrogenase, edited by Yoshida, A. and Beutler, E.Orlando, FL:Academic Press, Inc. 1986,p. 517-523. * Yoshida, A. and Lebo, R.V. Existence of glucose-6-phosphate dehydrogenase-like locus on chromosome 17. Am.J.Hum.Genet. 39:203-206, 1986. * Aksoy, K., Yuregir, G.T., Dikmen, N., and Unlukurt, I. Three new G6PD variants, G6PD Adana, G6PD Samandag, and G6PD Balcali in Cukurova, Turkey. Hum.Genet. 76:199-201, 1987. * Alayash, A.I., Dafallah, A., and Wilson, M.T. Glycosylated hemoglobin in Saudi sickle cell patients with glucose-6-phosphate dehydrogenase deficiency. Acta Haematol.(Basel) 78:54-56, 1987. * Anderson, B.B., Carandina, G., Lucci, M., Perry, G.M., and Vullo, C. Red-cell GSH regeneration and glutathione reductase activity in G6PD variants in the Ferrara area. Br.J.Haematol. 67:459-466, 1987. * Anderson, B.B., Clements, J.E., Perry, G.M., Studds, C., Vullo, C., and Salsini, G. Glutathione reductase activity and its

relationship to pyridoxine phosphate activity in G6PD deficiency. Eur.J.Haematol. 38:12-20, 1987. * Barenghi, L., Ceriotti, F., Ripamonti, M., Luzzana, M., and Bonini, P. Erythrocytic glucose-6-phosphate dehydrogenase measured by a differential pH technique. Clin.Chem. 33:579-582, 1987. * Baron, M., Risch, N., Hamburger, R., Mandel, B., Kushner, S., Newman, M., Drumer, D., and Belmaker, R.H. Genetic linkage between X-chromosome markers and bipolar affective illness. Nature 326:289-292, 1987. Notes: A pedigree study shows close linkage of bipolar affective illness (manic depression) to the X-chromosome markers colour blindness and glucose-6-phosphate dehydrogenase deficiency. The maximum lod score ranges from 7.52 (assuming homogeneity) to 9.17 (assuming heterogeneity); that is, the odds in favour of linkage range between 3 X 10(7) to 1 and 10(9) to 1. These results provide confirmation that a major psychiatric disorder can be caused by a single genetic defect. As a possible first step in characterizing the primary genetic abnormality, this finding may have important implications for the aetiology, nosology, pathophysiology and, possibly, prevention and treatment of bipolar affective disorder. It also provides a means for identifying and characterizing homogeneous populations of patients and may help in clarifying aetiological heterogeneity. * Barretto, O.C.O. and Nonoyama, K. Gd(+) Cuiaba, a new rare glucose-6-phosphate dehydrogenase variant presenting normal activity. Hum.Genet. 77:201-202, 1987. * Beutler, E. and Lind, S. Unpublished , 1987. Notes: G 6 PD Lynn. Patient Kudzi. * Beutler, E. Glucose-6-phosphate dehydrogenase deficiency. In: Clinical Studies in Medical Biochemistry, edited by Glew, R.H. and Peters, S.P.New York:Oxford University Press, 1987, Notes: MS121 (B759). * Beutler, E., Frenkel, E.P., and Forman, L. Unpublished , 1987. Notes: G-6-PD Dallas. Patient-- Mark Bennet. * Bhadbhade, M.M., Adams, M.J., Flynn, T.G., and Levy, H.R. Sequence identity between a lysine-containing peptide from Leuconostoc mesenteroides glucose-6-phosphate dehydrogenase and an active site peptide from human erythrocyte glucose-6-phosphate dehydrogenase. FEBS Lett. 211:243-246, 1987. * Bresolin, N., Bet, L., Moggio, M., Meola, G., Comi, G., Gilardi, A., and Scarlato, G. Muscle G6PD deficiency. Lancet 2:212-213, 1987. * El-Hazmi, M.A.F. and Warsy, A.S. Interaction between glucose-6-phosphate dehydrogenase deficiency and sickle cell gene in Saudi Arabia. Trop.Geogr.Med. 39:32-35, 1987. * El-Hazmi, M.A.F. and Warsy, A.S. A normal reference range for erythrocyte glucose-6-phosphate dehydrogenase in a Saudi population. Med.Lab.Sci. 44:125-129, 1987. * Fialkow, P.J., Singer, J.W., Raskind, W.H., Adamson, J.W., Jacobson, R.J., Bernstein, I.D., Dow, L.W., Najfeld, V., and Veith, R. Clonal development, stem-cell differentiation, and clinical remissions in acute nonlymphocytic leukemia. N.Engl.J.Med. 317:468-473, 1987. * Frigerio, R., Sole, G., Olla, N., Lovicu, M., Passiu, G., and Carcassi, U. G-6-PD Cagliari II: A new G-6-PD variant. Haematologica (Pavia) 72:241-243, 1987. * Gutierrez, A., Garcia, M., Estrada, M., Quintero, I., and Gonzalez, R. Glucose-6-phosphate dehydrogenase (G6PD) Guantanamo

and G6PD Caujeri: Two new glucose-6-phosphate dehydrogenase-deficient variants found in Cuba. Biochem.Genet. 25:231-238, 1987. * Hansen, R.J. and Jungermann, K. Sex differences in the control of glucose-6-phosphate dehydrogenase: Interaction of estrogen, testosterone and insulin in the regulation of enzyme levels in vivo and in cultured hepatocytes. Biol.Chem.Hoppe Seyler 368:955-962, 1987. * Hidalgo, C.P.C., Gonzalez, O.L., Rodrguez, M., and Castellanos, T. Analisis del polimorfismo genetico de la G-6FD eritrocitaria en la region central de Cuba. Medicentro 3:149-157, 1987. * Jackson, L.C. Animal source for human G6PD isozymes GdA and GdB. Biochem.Med.Metab.Biol. 38:125, 1987. * Jacobasch, G., Buckwitz, D., Jurowski, R., Gerth, C., Plonka, A., and Kuckelkorn, U. Heterogeneity of glucose-6-phosphate dehydrogenase enzymopathies in the GDR. Biomed.Biochim.Acta 46:177-181, 1987. Notes: G6PD variants of 13 patients from 12 German families with different clinical symptoms have been characterized kinetically. Vmax G6PD was nearly zero in red blood cells of all carriers. Therefore G6PD variants were isolated from leucocytes, which proved to be a suitable source for analysis of instable G6PD variants. The testing program included KmG6P, KmNADP, Ki values of NADPH, ATP and 2,3 P2G, rate of utilization of dG6P, Gal6P, dNADP, NAD, and pH dependence. From the results obtained one can conclude that all analyzed G6PD variants represent individual mutations. The degree of metabolic dysregulation can be explained by the different kinetic and physico-chemical properties of these G6PD variants. * Knox-Macaulay, H.H.M. Glucose-6-phosphate dehydrogenase deficiency in blood donors. Saudi Med.J. 8:325-326, 1987. * Kumakawa, T., Suzuki, S., Fujii, H., and Miwa, S. Frequency of glucose 6-phosphate dehydrogenase (G6PD) deficiency in Tokyo and a new variant: G6PD Musashino. Acta Haematol.Jpn. 50:25-28, 1987. * Leung, A.K. Screening of jaundiced neonates for glucose-6-phosphate dehydrogenase deficiency. South Med.J. 80:217-218, 1987. Notes: Glucose-6-phosphate dehydrogenase (G6PD) deficiency is transmitted as an X-linked recessive disorder, and thus female infants are expected to be only rarely affected. Review of the records of 1,478 jaundiced newborn infants (728 boys and 750 girls) screened for G6PD deficiency at the Foothills Provincial Hospital in Calgary showed 41 (5.6%) boys and 17 (2.2%) girls with this disorder. In view of the unexpected and unexplained high frequency of G6PD deficiency in female infants, I recommend that screening for this disorder be done in selected jaundiced infants regardless of sex. * Mamlok, R.J., Mamlok, V., Mills, G.C., Daeschner, C.W.,III, Schmalstieg, F.C., and Anderson, D.C. Glucose-6-phosphate dehydrogenase deficiency, neutrophil dysfunction and Chromobacterium violaceum sepsis. J.Pediatr. 111:852-854, 1987. Notes: G6PD Beaumont. * Markowitz, N. and Saravolatz, L.D. Use of trimethoprim-sulfamethoxazole in a glucose-6-phosphate dehydrogenase-deficient population. Rev.Infect.Dis. 9 Suppl 2:S218-S229, 1987. Notes: Trimethoprim-sulfamethoxazole (TMP-SMZ) has been associated with hemolytic anemia in patients deficient in

glucose-6-phosphate dehydrogenase (G-6-PD). The effect of a daily dose of SMZ of 50 mg/kg was evaluated in a double-blinded study that compared vancomycin with TMP-SMZ given intravenously for treatment of serious Staphylococcus aureus infections. Levels of G-6-PD were determined when patients entered the trial. Most patients were black Americans. G-6-PD- deficient patients were followed serially, with determinations of hemoglobin, haptoglobin, and bilirubin levels, reticulocyte count, and urinalysis. Pretherapy hemoglobin levels were compared with levels during and after therapy. One hundred patients were divided into four groups: group A comprised G-6-PD-deficient patients receiving TMP-SMZ (n = 20); group B, G-6-PD-deficient patients receiving vancomycin (n = 25); and groups C and D, patients with normal G-6-PD levels receiving TMP-SMZ (n = 24) and vancomycin (n = 31), respectively. Groups we * Meier, W., Lerche, D., Jacobasch, G., and Paulitschke, M. Membrane elastic shear modulus of red blood cells with glucose-6phosphate dehydrogenase and pyruvatekinase enzymopathies. Int.J.Microcirc.Clin.Exp. 5:297-302, 1987. Notes: The membrane elastic shear modulus mu determined by a micropipette technique was found to be elevated by 25% to 200% for red blood cells (RBC) from 7 patients with glucose-6-phosphate dehydrogenase (G-6-PD) and 9 patients with pyruvate-kinase (PK) enzymopathies above the mean value for normal controls. All patients exhibit chronic nonspherocytic hemolytic anemias. A negative linear correlation (r = - 0.72) between mu and the number of reticulocytes was obtained in G-6-PD deficiencies. In contrast, a positive correlation (r = 0.88) was found for red blood cells of patients with PK deficiency. A mechanically induced swelling of RBC was observed for some deficient cells. The results are discussed in the framework of structural alterations of the RBC membrane due to the disturbed pentose- phosphate pathway and the diminished ATP supply through glycolysis, respectively. * Mohrenweiser, H.W. Functional hemizygosity in the human genome: direct estimate from twelve erythrocyte enzyme loci. Hum.Genet. 77:241-245, 1987. * Ninfali, P., Palma, F., and Fornaini, G. Rabbit bone marrow glucose-6-phosphate dehydrogenase during erythroid cell development. Mol.Cell.Biochem. 75:85-92, 1987. * Oberle, I., Camerino, G., Wrogemann, K., Arveiler, B., Hanauer, A., Raimondi, E., and Mandel, J.L. Multipoint genetic mapping of the Xq26-q28 region in families with fragile X mental retardation and in normal families reveals tight linkage of markers in q26-q27. Hum.Genet. 77:60-65, 1987. Notes: The q26-q28 region of the human X chromosome contains several important disease loci, including the locus for the fragile X mental retardation syndrome. We have characterized new polymorphic DNA markers useful for the genetic mapping of this region. They include a new Bell restriction fragment length polymorphism (RFLP) detected by the probe St14-1 (DXS52) and which may therefore be of diagnostic use in hemophilia A families. A linkage analysis was performed in fragile X families and in large normal families from the Centre d'Etude du Polymorphisme Humain (CEPH) by using seven polymorphic loci located in Xq26-q28. This multipoint linkage study allowed us to establish the order centromere-DXS100-DXS86-DXS144-DXS51-F9-FRAX+ ++-(DXS52-DXS15). Together with other studies, our results define a cluster of nine loci that are located in Xq26-q27 and map within a 10 to 15 centimorgan region. This contrasts with the

paucity of markers (other than the fragile X locus) between the F9 gene in q27 and the G6PD cl * Oliver, C.N., Ahn, B., Moerman, E.J., Goldstein, S., and Stadtman, E.R. Age-related changes in oxidized proteins. J.Biol.Chem. 262:5488-5491, 1987. * Ravindranath, Y. and Beutler, E. Two new variants of glucose-6-phosphate dehydrogenase associated with congenital non-spherocytic hemolytic anemia: G6PD Wayne and G6PD Huron. Am.J.Hematol. 24:357-363, 1987. Notes: (B754) Wayne patient-- Scott Henry. Huron patient-- Jason Booms. * Takizawa, T. and Yoshida, A. Molecular abnormality of the common glucose-6-phosphate dehydrogenase variant, G6PD A(+), and restriction-fragment-length polymorphism. Am.J.Hum.Genet. 41:A241, 1987. * Takizawa, T., Yoneyama, Y., Miwa, S., and Yoshida, A. A single nucleotide base transition is the basis of the common human glucose-6-phosphate dehydrogenase variant A(+). Genomics 1:228-231, 1987. * Thorburn, D.R. and Kuchel, P.W. Computer simulation of the metabolic consequences of the combined deficiency of 6-phosphogluconolactonase and glucose-6-phosphate dehydrogenase in human erythrocytes. J.Lab.Clin.Med. 110:70-74, 1987. * Verma, C., Wijnen, J.T., and Khan, P.M. G6PD Punjab, a dialysis sensitive variant of human glucose-6-phosphate dehydrogenase. J.Genet. 66:17-24, 1987. * Warsy, A.S. and El-Hazmi, M.A.F. Glucose-6-phosphate dehydrogenase deficiency in Saudi Arabia - A review. Saudi Med.J. 8:12-20, 1987. * White, B.J. and Levy, H.R. Modification of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides with the 2',3'-dialdehyde derivative of NADP+ (oNADP+). J.Biol.Chem. 262:1223-1229, 1987. Notes: Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides is irreversibly inactivated by the 2,3'-dialdehyde of NADP+ (oNADP+) in the absence of substrate. The inactivation is first order with respect to NADP+ concentration and follows saturation kinetics, indicating that the enzyme initially forms a reversible complex with the inhibitor followed by covalent modification (KI = 1.8 mM). NADP+ and NAD+ protect the enzyme from inactivation by oNADP+. The pK of inactivation is 8.1. oNADP+ is an effective coenzyme in assays of glucose-6-phosphate dehydrogenase (Km = 200 microM). Kinetic evidence and binding studies with [14C] oNADP+ indicate that one molecule of oNADP+ binds per subunit of glucose-6-phosphate dehydrogenase when the enzyme is completely inactivated. The interaction between oNADP+ and the enzyme does not generate a Schiff's base, or a conjugated Schiff's base, but the data are consistent with the formation of a dihydroxymorpholino derivative. * Wolf, B.H.M., Weening, R.S., Schutgens, R.B.H., van Noorden, C.J.F., Vogels, I.M.C., and Nagelkerke, N.J.D. Detection of glucose-6-phosphate dehydrogenase deficiency in erythrocytes: a spectrophotometric assay and a fluorescent spot test compared with a cytochemical method. Clin.Chim.Acta 168:129-136, 1987. * Wong, C.T. and Saha, N. Haemoglobin, serum iron, transferrin, ferritin concentrations and total iron-binding capacity in erythrocyte glucose-6-phosphate dehydrogenase deficiency. Trop.Geogr.Med. 39:350-353, 1987. * Yoshida, A. and Roth, E.F.,Jr. Glucose-6-phosphate dehydrogenase of malaria parasite Plasmodium falciparum. Blood

69:1528-1530, 1987. * Zimran, A., Torem, S., and Beutler, E. The in vivo ageing of red cell enzymes: Direct evidence of biphasic decay from polycythemic rabbits with reticulocytosis. Clin.Res. 35:604A, 1987. (Abstract) Notes: (B790). * Abkowitz, J.L., Ott, R.M., Holly, R.D., and Adamson, J.W. Clonal evolution following chemotherapy-induced stem cell depletion in cats heterozygous for glucose-6-phosphate dehydrogenase. Blood 71:1687-1692, 1988. * Agarwal, S., Gupta, U.R., Gupta, R.C., Anand, N., and Agarwal, S.S. Susceptibility of glucose-6-phosphate dehydrogenase deficient red cells to primaquine enantiomers and two putative metabolites--I. Effect on reduced glutathione, methemoglobin content and release of hemoglobin. Biochem.Pharmacol. 37:4605-4609, 1988. * Barraviera, B., Mendes, R.P., Pereira, P.C., Machado, J.M., Curi, P.R., and Meira, D.A. Measurement of glucose-6-phosphate dehydrogenase and glutathione reductase activity in patients with paracoccidioidomycosis treated with ketoconazole. Mycopathologia 104:87-91, 1988. Notes: Hemoglobin rates, hematocrit and glucose-6-phosphate dehydrogenase (G6PD) and glutathione reductase activities were measured in 38 patients with paracoccidioidomycosis treated with ketoconazole or sulfadoxin, and in 13 normal individuals. Ketoconazole-treated patients showed reduced G6PD and glutathione reductase activities. One of these patients was found to be G6PD-deficient and suffered a hemolytic episode during treatment, which, however, did not require interruption of therapy. The authors suggest that patients showing an erythrocyte enzyme defect should be monitored hematologically during treatment with ketoconazole. They also suggest that ketoconazole is an oxidant drug in addition to being a possible inhibitor of antioxidant erythrocyte enzymes. * Bashan, N., Peleg, N., and Moses, S.W. Attempts to predict the hemolytic potential of drugs in glucose-6-phosphate dehydrogenase deficiency of the Mediterranean type by an in vitro test. Isr.J.Med.Sci. 24:61-64, 1988. * Bautista, J.M., Garrido, A., and Soler, G. Effect of NADP+ and NADPH on controlled tryptic cleavage of glucose-6-phosphate dehydrogenase from Dicentrarchus labrax (bass) liver. Biochem.Soc.Trans. 16:903-904, 1988. * Beamont, A.H., Miguel, A., Goos, C.M., Vermeesch-Markslag, A.M., Hermans, A., and Vermorken, A.J. The suitability of saliva for detection of glucose-6-phosphate dehydrogenase deficiency University of Nijmegen, The Netherlands. Mol.Biol.Rep. 13:73-78, 1988. Notes: Saliva was investigated for its suitability as a biopsy tissue for the determination of glucose-6-phosphate dehydrogenase deficiency. It appears that there is a significant difference between the activity of the enzyme in patients and controls. However, some controls have very low values making discrimination between patients and controls using a qualitative method impossible. Glucose-6-phosphate dehydrogenase deficiency is a relevant clinical problem in many rural areas in developing countries. Existing methods for determination of the deficiency in blood and hair follicles do not meet the criteria necessary for their large scale introduction in the areas of the world that are concerned by the problem. The present study shows that saliva is not a suitable alternative. Between the three biopsy tissues

compared: blood, hair follicles and saliva, hair follicles remain most attractive since their isolation hardly involves the risk of infection. A simplified method for the detection of glucose-6-phospha * Beutler, E. and Yoshida, A. Genetic variation of glucose-6-phosphate dehydrogenase: A catalog and future prospects. Medicine (Baltimore) 67:311-334, 1988. Notes: (B789). * Beutler, E. Anemia, aspirin, and ancestry. JAMA 259:2467, 1988. Notes: (B775). * Beutler, E., Forman, L., and Miale, T. Unpublished , 1988. Notes: G6PD Springfield from Dr. Miale. Pt. Aaron Rubenacker. * Beutler, E., Gelbart, T., and Forman, L. Unpublished , 1988. Notes: G6PD Beverly Hills Pt. Mosso. * Camardella, L., Caruso, C., Rutigliano, B., Romano, M., Di Prisco, G., and Descalzi-Cancedda, F. Human erythrocyte glucose-6-phosphate dehydrogenase: Identification of a reactive lysyl residue labelled with pyridoxal 5'-phosphate. Eur.J.Biochem. 171:485-489, 1988. * Chaves, M., S enz, G.F., Quintana, E., Montero, A., and Jimenez, J. Polymorphism of erythrocytic glucose-6-phosphate dehydrogenase in Costa Rica. Sangre (Barc.) 33:12-14, 1988. * Csepreghy, M., Yeilding, A., Lilly, M., Scott, C.W., and Prchal, J.T. Characterization of a new glucose-6-phosphate dehydrogenase variant: G6PD Central City. Am.J.Hematol. 28:61-62, 1988. * D'Urso, M., Luzzatto, L., Perroni, L., Ciccodicola, A., Gentile, G., Peluso, I., Persico, M.G., Pizzella, T., Toniolo, D., and Vulliamy, T.J. An extensive search for RFLP in the human glucose-6-phosphate dehydrogenase locus has revealed a silent mutation in the coding sequence. Am.J.Hum.Genet. 42:735-741, 1988. * Dessi, S., Batetta, B., Cherchi, R., Onnis, R., Pisano, M., and Pani, P. Hexose monophosphate shunt enzymes in lung tumors from normal and glucose-6-phosphate-dehydrogenase-deficient subjects. Oncology 45:287-291, 1988. Notes: Glucose-6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate, dehydrogenase the key enzymes of the hexose monophosphate shunt pathway, were measured in both surrounding and tumoral lung tissues from normal and G6PD-deficient subjects. A significant increase of these enzymatic activities in tumoral tissue was found not only in G6PD-normal patients, but also in G6PD-deficient patients with very low or nonmeasurable G6PD activity in both erythrocytes and normal lung tissue. * Du, C.S., Xu, Y.K., Hua, X.Y., Wu, Q.L., and Liu, L.B. Glucose-6-phosphate dehydrogenase variants and polymorphic frequency in Guangdong, China. Hum.Genet. 80:385-388, 1988. Notes: New G-6-PD variants with the names Huazhou, Boluo, Boluo-2, Gaomin, Kaiping, Guangzhou, Qing-Baijiang, Gaozhou. * El-Alfy, M.S., Khalifa, A.S., Mokhtar, G., Fakeri, A.A., Khazhak, M.A., El-Baz, F., and El-Kholy, M. Effect of desferrioxamine (DF) on hemolysis in glucose-6-phosphate dehydrogenase (G6PD) deficiency. Blood 72 (Suppl 1):40A, 1988. (Abstract) * el-Hazmi, M.A. and Warsy, A.S. Correlation between red cell glucose-6-phosphate dehydrogenase level and haematological parameters. Med.Lab.Sci. 45:255-260, 1988. * El-Hazmi, M.A.F. and Warsy, A.S. Glucose-6-phosphate

dehydrogenase deficiency in Saudi Arabia. A study in Al-Ula. Hum.Hered. 38:317-322, 1988. * Eldamhougy, S., Elhelw, Z., Yamamah, G., Hussein, L., Fayyad, I., and Fawzy, D. The vitamin E status among glucose-6 phosphate dehydrogenase deficient patients and effectiveness of oral vitamin E. Int.J.Vitam.Nutr.Res. 58:184-188, 1988. Notes: The effect of oral vitamin E therapy (800 IU/day) on correcting haematologic variables and on raising the plasma vitamin E level among glucose-6 phosphate dehydrogenase deficient subjects with history of hemolysis was studied. After 16 week period there was a positive response to vitamin E administration presented by sustained improvement in blood hemoglobin and plasma vitamin E concentrations. In the meanwhile, the vitamin E supplementation led to reduced reticulocytosis and control % hemolysis. * Ferraris, A.M., Broccia, G., Meloni, T., Forteleoni, G., and Gaetani, G.F. Glucose-6-phosphate dehydrogenase deficiency and incidence of hematologic malignancy. Am.J.Hum.Genet. 42:516-520, 1988. * Forteleoni, G., Argiolas, L., Farris, A., Ferraris, A.M., Gaetani, G.F., and Meloni, T. G6PD deficiency and breast cancer. Tumori 74:665-667, 1988. * Fouts, D., Ganguly, R., Gutierrez, A.G., Lucchesi, J.C., and Manning, J.E. Nucleotide sequence of the Drosophila glucose-6-phosphate dehydrogenase gene and comparison with the homologous human gene. Gene 63:261-275, 1988. * Gaetani, G.F. and Ferraris, A.M. Recent developments on Mediterranean G6PD. Br.J.Haematol. 68:1-2, 1988. * Hall, K., Schreeder, M.T., and Prchal, J.T. G6PD Huntsville: A new glucose-6-phosphate dehydrogenase associated with chronic hemolytic anemia. Hum.Genet. 79:90-91, 1988. * Hirono, A. and Beutler, E. Molecular cloning and nucleotide sequence of cDNA for human glucose-6-phosphate dehydrogenase variant A(-). Proc.Natl.Acad.Sci.USA 85:3951-3954, 1988. Notes: (B777). * Hirono, A., Vives-Corrons, J.L., Johnson, C., Prchal, J., Kuhl, W., and Beutler, E. The molecular biology of electrophoretically fast, deficient glucose-6-phosphate dehydrogenase variants. Blood 72 (Suppl 1):44A, 1988. (Abstract) Notes: (B795). * Hirono, A. and Beutler, E. The common G6PD A(-) mutation arose in a G6PD A(+) individual. Clin.Res. 36:561A, 1988. (Abstract) Notes: (B772). * Ho, Y.-S., Howard, A.J., and Crapo, J.D. Cloning and sequence of a cDNA encoding rat glucose-6-phosphate dehydrogenase. Nucleic Acids Res. 16:7746, 1988. * Hochstein, P. Perspectives on hydrogen peroxide and drug-induced hemolytic anemia in glucose-6-phosphate dehydrogenase deficiency. J.Free Radical Biol.Med. 5:387-392, 1988. * Jeffery, J., Sderling-Barros, J., Murray, L.A., Hansen, R.J., Szepesi, B., and Jrnvall, H. Molecular diversity of glucose-6-phosphate dehydrogenase: Rat enzyme structure identifies NH2-terminal segment, shows initiation from sites nonequivalent in different organisms, and establishes otherwise extensive sequence conservation. Proc.Natl.Acad.Sci.USA 85:7840-7843, 1988. * Kanno, H., Takano, T., Fujii, H., Tani, K., Morisaki, T., Hirono, A., Kumakawa, T., Ogura, H., Takahashi, K., Tsutsumi, H.,

and Miwa, S. A new glucose-6-phosphate variant (G6PD Iwate) associated with congential non-spherocytic hemolytic anemia. Acta Haematol.Jpn. 51:715-719, 1988. * Kurlandsky, S.B., Hilburger, A.C., and Levy, H.R. Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides: Ligand-induced conformational changes. Arch.Biochem.Biophys. 264:93-102, 1988. * Leung, A.K.C. and McLeod, D.R. Prevalence of glucose-6-phosphate dehydrogenase deficiency. J.Pediatr. 112:1051-1052, 1988. * Llobell, A., Lopez-Ruiz, A., Peinado, J., and Lopez-Barea, J. Glutathione reductase directly mediates the stimulation of yeast glucose-6-phosphate dehydrogenase by GSSG. Biochem.J. 249:293-296, 1988. * Luzzatto, L. The genetic basis of blood cell enzymopathies. In: Proceedings of the XXII Congress of the International Society of Hematology,Anonymous Milan:International Society of Hematology, 1988,p. 63-70. * Mason, P.J., Vulliamy, T.J., Foulkes, N.S., Town, M., Haidar, B., and Luzzatto, L. The production of normal and variant human glucose-6-phosphate dehydrogenase in cos cells. Eur.J.Biochem. 178:109-113, 1988. * Mela, Q., Perpignano, G., Ruggiero, V., and Longatti, S. Tolerability of tiaprofenic acid in patients with glucose-6-phosphate dehydrogenase (G6PD) deficiency. Drugs 35:107-110, 1988. Notes: Glucose-6-phosphate dehydrogenase (G6PD) deficiency is an X-linked genetic disorder which can lead to acute haemolytic anaemia following ingestion of fava beans and the administration of certain drugs, mainly in subjects with bacterial or viral infections. It is common in the Mediterranean region and many variants are found in Sardinia. The aim of this study was to evaluate in vivo if treatment with tiaprofenic acid 600 mg daily for 15 days would reduce erythrocyte GSH (reduced glutathione) concentrations and thus produce erythrocytolysis (assessed by evaluation of 51Cr-labelled erythrocyte survival) in subjects with G6PD deficiency. GSH concentrations were also evaluated in vitro after incubation of G6PD-deficient erythrocytes with increasing doses of tiaprofenic acid (20, 50, 100, 150 and 200 mg/L) and with acetylphenylhydrazine 5 mg. The results obtained both in vitro and in vivo confirmed the absence of any oxidative action of tiaprofenic acid on the erythrocytes of G6PD-deficient subjects. * Motulsky, A.G. Normal and abnormal color-vision genes. Am.J.Hum.Genet. 42:405-407, 1988. * Obukowicz, M.G., Turner, M.A., Wong, E.Y., and Tacon, W.C. Secretion and export of IGF-1 in Escherichia coli strain JM101 MO 63198. Mol.Gen.Genet. 215:19-25, 1988. * Ogura, H., Morisaki, T., Tani, K., Kanno, H., Tsutsumi, H., Takahashi, K., Miyamori, T., Fujii, H., and Miwa, S. A new glucose-6-phosphate dehydrogenase variant (G6PD Tsukui) associated with congenital hemolytic anemia. Hum.Genet. 78:369-371, 1988. Notes: A new glucose-6-phosphate dehydrogenase (G6PD) variant associated with chronic nonspherocytic hemolytic anemia was found in a 20-year-old Japanese male who showed mild hemolysis after an upper respiratory tract infection. The patient had been noted to have jaundice and reticulocytosis several times before this episode. The enzyme activity of the variant was 1.5% of normal. The enzymatic characteristics were slow anodal electrophoretic

mobility, high Km G6P, normal Km NADP, decreased heat stability, and a normal pH optimum. From these results, the enzyme was considered to be a new class 1 variant and was designated G6PD Tsukui. * Poon, M.-C., Hall, K., Scott, C.W., and Prchal, J.T. G6PD Viangchan: A new glucose 6-phosphate dehydrogenase variant from Laos. Hum.Genet. 78:98-99, 1988. * Prchal, J.T., Hall, K., Csepreghy, M., Lilly, M., Berkow, R., and Scott, C.W. Two apparent glucose-6-phosphate dehydrogenase variants in normal XY man: G6PD Alabama. Am.J.Med. 84:517-523, 1988. * Pretsch, W., Charles, D.J., and Merkle, S. X-linked glucose-6-phosphate dehydrogenase deficiency in Mus musculus. Biochem.Genet. 26:89-103, 1988. Notes: A mouse with X-linked glucose-6-phosphate dehydrogenase (G6PD) deficiency has been recovered in offspring of 1-ethyl-1-nitrosourea-treated male mice. The activity alteration was detected in blood but can also be observed in other tissue extracts. Hemizygous, heterozygous, and homozygous mutants have, respectively, about 15, 60, and 15% G6PD remaining activity in the blood as compared to the wild type. Erythrocyte indices did not show differences between mutants and wild types. The mutation does not affect the electrophoretic migration, the isoelectric point, or the thermal stability. Kinetic properties, such as the Km for glucose-6-phosphate or for NADP and the relative utilization of substrate analogues, showed no differences between wild types and mutants with the exception of the relative utilization of deamino-NADP which was significantly lower in mutants. This is presently the only animal model for X-linked G6PD deficiency in humans. * Renner, H., Michel, P., and Solem, E. Detection of glucose-6-phosphate dehydrogenase-deficient heterozygotes: Cytochemical method and spectrophotometric assay. Clin.Chim.Acta 174:239-240, 1988. * Rosenbloom, B.E., Weingarten, S., Rosenfelt, F.P., and Weinstein, I.M. Severe hemolytic anemia due to glucose-6-phosphate dehydrogenase deficiency and Epstein-Barr virus infection. Mt.Sinai J.Med. 55:404-405, 1988. * Roth, E.,Jr. and Schulman, S. The adaptation of Plasmodium falciparum to oxidative stress in G6PD deficient human erythrocytes. Br.J.Haematol. 70:363-367, 1988. * Steinberg, M.H., West, M.S., Gallagher, D., Mentzer, W.C.J., and The cooperative study of sickle cell diseases Effects of glucose-6-phosphate dehydrogenase deficiency upon sickle cell anemia. Blood 71:748-752, 1988. * Thomas, G.A., Williams, D., and Williams, E.D. The demonstration of tissue clonality by X-linked enzyme histochemistry. J.Pathol. 155:101-108, 1988. * Toniolo, D., Martini, G., Migeon, B.R., and Dono, R. Expression of the G6PD locus on the human X chromosome is associated with demethylation of three CpG islands within 100 kb of DNA. EMBO J. 7:401-406, 1988. * Vulliamy, T.J., D'Urso, M., Battistuzzi, G., Estrada, M., Foulkes, N.S., Martini, G., Calabro, V., Poggi, V., Giordano, R., Town, M., Luzzatto, L., and Persico, M.G. Diverse point mutations in the human glucose 6-phosphate dehydrogenase gene cause enzyme deficiency and mild or severe hemolytic anemia. Proc.Natl.Acad.Sci.USA 85:5171-5175, 1988. * Williams, C.K.O., Osotimehin, B.O., Ogunmola, G.B., and Awotedu, A.A. Haemolytic anaemia associated with Nigerian

barbecued meat (red suya). Afr.J.Med.Med.Sci. 17:71-75, 1988. Notes: Five cases of haemolytic anaemia occurring in male Nigerians following the ingestion of spiced barbecued meat (suya) are described. Although suya is a popular food item in various parts of Nigeria, all five patients described in this report had consumed a special brand, called red suya, purchased from vendors at a popular road junction between the cities of Lagos and Ibadan. Ingestion of the culprit suya sample was followed within 24 h by malaise and fever, while passage of dark-coloured urine and jaundice followed 1-3 days thereafter. Glucose-6-phosphate dehydrogenase (G6PD) deficiency was demonstrated by a fluorescent screening test in all cases, while the enzyme phenotype was shown to be GdA- in all four cases studied by starch-gel electrophoresis, thus suggesting that G6PD deficiency was a predisposing factor in the cases reported in this series. The haemolytic disease was self-limiting and full recovery followed in all cases. In view of the markedly circumscribed range from where the patients o * Wolf, B.H.M., Schutgens, R.B.H., Nagelkerke, N.J.D., and Weening, R.S. Glucose-6-phosphate dehydrogenase deficiency in ethnic minorities in the Netherlands. Trop.Geogr.Med. 40:322-330, 1988. * Yoshida, A., Takizawa, T., and Prchal, J.T. RFLP of the X chromosome-linked glucose-6-phosphate dehydrogenase locus in Blacks. Am.J.Hum.Genet. 42:872-876, 1988. * Yoshida, A. and Takizawa, T. The same extra Fokl cleavage site exists in glucose-6-phosphate dehydrogenase variants A(+) and A(-). Am.J.Hum.Genet. 43:131-133, 1988. * Zhdanova, N.S., Pack, S.D., Mazurok, N.A., Nesterova, T.B., Gradov, A.A., and Serov, O.L. Subchromosomal localization and order of GLA, PGK1, HPRT, and G6PD loci on the X chromosome of the American mink (Mustela vison). Cytogenet.Cell Genet. 48:2-5, 1988. * Abu-Osba, Y.K., Mallouh, A.A., and Hann, R.W. Incidence and causes of sepsis in glucose-6-phosphate dehydrogenase-deficient newborn infants. J.Pediatr. 114:748-752, 1989. * Alayash, A.I., Bonaventura, J., and Al-Quorain, A. A benign sickle-cell disease in a Saudi subject with Beta0-thalassemia and glucose-6-phosphate dehydrogenase deficiency. Hum.Hered. 39:118-120, 1989. * Beutler, E., Forman, L., Gelbart, T., and LeGrand, S.B. Unpublished , 1989. Notes: G 6 PD Gastonia. Patient Danny C. Silcox, Gastonia, N.C. Dr. Susan B. LeGrand. * Beutler, E., Hirono, A., and Kuhl, W. Definition of the NADP-binding domain of glucose-6-phosphate dehydrogenase (G6PD) by sequence analysis of mutants. Blood 74:140A, 1989. Notes: (B818). * Beutler, E., Kuhl, W., Vives-Corrons, J.-L., and Prchal, J.T. Molecular heterogeneity of G6PD A-. Blood 74:2550-2555, 1989. Notes: (B822). * Beutler, E., Vives-Corrons, J.L., Hirono, A., Prchal, J.T., and Crader, W. The molecular biology of variation in glucose-6-phosphate dehydrogenase. In: The Red Cell: Seventh Ann Arbor Conference, edited by Brewer, G.J.New York:Alan R. Liss, Inc. 1989,p. 39-54. Notes: (B821). * Beutler, E., Gelbart, T., Forman, L., and Fairbanks, V.F. Unpublished , 1989.

Notes: G6PD Tomah. Pt=Drinkwine. Physician=V.F.Fairbanks. * Beutler, E., Forman, L., and Jackman, R. Unpublished , 1989. Notes: G6PD Marion; Patient=David Groves; Physician=Roger Jackman. * Beutler, E. Evolution of glucose-6-phosphate dehydrogenase variants A+ and A-. Response. Blood 74:1860-1861, 1989. Notes: (B826). * Beutler, E. Glucose-6-phosphate dehydrogenase: New perspectives. Blood 73:1397-1401, 1989. Notes: (B806). * Beutler, E., Gelbart, T., Forman, L., and Winkelmann, J. Unpublished , 1989. Notes: G6PD Minnesota. Patient=Robin Gault;Physician=John Winkelmann. * Birke, S., Kim, H.W., Periclou, A., Schorsch, B., Grouse, D., and Craney, C. Kinetics of human erythrocyte glucose-6-phosphate dehydrogenase dimers. Biochim.Biophys.Acta 999:243-247, 1989. * Bresolin, N., Bet, L., Moggio, M., Meola, G., Fortunato, F., Comi, G., Adobbati, L., Geremia, L., Pittalis, S., and Scarlato, G. Muscle glucose-6-phosphate dehydrogenase deficiency. J.Neurol. 236:193-198, 1989. * Buckwitz, D., Jacobasch, G., Kuckelkorn, U., Plonka, A., and Gerth, C. Glucose-6-phosphate dehydrogenase from Plasmodium berghei: Kinetic and electrophoretic characterization. Unpublished , 1989. * Cherian, M. and Rawal, U.M. Effect of busulfan on crystalline lens--Glutathione, glutathione reductase and glucose-6-phosphate dehydrogenase. Indian J.Exp.Biol. 27:915-916, 1989. * Chiba, Y., Takizawa, S., Kishi, K., Hattori, A., Shibata, A., Matsumoto, N., Fujii, J., and Miwa, S. A new glucose 6-phosphate dehydrogenase (G6PD) variant (G6PD Niigata) with chronic hemolysis and liver hemochromatosis. Jpn.J.Int.Med. 78:41-47, 1989. * Chongxing, N., Shuntao, T., and Daixiong, C. Determination of glucose-6-phosphate dehydrogenase isoenzymes of human erythrocytes by a thin-layer PAG-IEF procedure. J.Lab.Clin.Med. 114:152-162, 1989. * Cocco, P., Dessi, S., Avataneo, G., Picchiri, G., and Heinemann, E. Glucose-6-phosphate dehydrogenase deficiency and cancer in a Sardinian male population: A case-control study. Carcinogenesis 10:813-816, 1989. * Csepreghy, M., Hall, M.K., Berkow, R.L., Jackson, S., and Prchal, J.T. Characterization of a new G6PD variant: G6PD Titusville. Am.J.Med.Sci. 297:114-117, 1989. * De Vita, G., Alcalay, M., Sampietro, M., Cappellini, M.D., Fiorelli, G., and Toniolo, D. Two point mutations are responsible for G6PD polymorphism in Sardinia. Am.J.Hum.Genet. 44:233-240, 1989. * Dhur, A., Galan, P., and Hercberg, S. Effects of different degrees of iron deficiency on cytochrome P450 complex and pentose phosphate pathway dehydrogenases in the rat. J.Nutr. 119:40-47, 1989. * Eanes, W.F., Ajioka, J.W., Hey, J., and Wesley, C. Restriction-map variation associated with the G6PD polymorphism in natural populations of Drosophila melanogaster. Mol.Biol.Evol. 6:384-397, 1989. * El-Hazmi, M.A.F. and Warsy, A.S. The effects of

glucose-6-phosphate dehydrogenase deficiency on the haematological parameters and clinical manifestations in patients with sickle cell anaemia. Trop.Geogr.Med. 41:52-56, 1989. * El-Hazmi, M.A.F. and Warsy, A.S. Frequency of glucose-6-phosphate dehydrogenase phenotypes and deficiency in Al-Baha. Hum.Hered. 39:313-317, 1989. * Farag, R.M., Gunaid, A.A., and Qirbi, A.A. Effect of khat on the metabolism of erythrocytes. Biochem.Pharmacol. 38:563-566, 1989. * Figueiredo, M.S., Pinto, B.O., and Zago, M.A. Dapsone-induced haemolytic anaemia and agranulocytosis in a patient with normal glucose-6-phosphate-dehydrogenase activity. Acta Haematol.(Basel) 82:144-145, 1989. * Fiorelli, G., Manoussakis, C., Sampietro, M., Pittalis, S., Guglielmino, C.R., and Cappellini, M.D. Different polymorphic variants of glucose-6-phosphate dehydrogenase (G6PD) in Italy. Ann.Hum.Genet. 53:229-236, 1989. * Gerhartz, H.H., Mittermuller, J., and Kulozik, A. Anemia requiring transfusion and amenorrhea in a 23-year-old patient desiring children. Internist (Berlin) 30:258-262, 1989. * Gulati, S., Singh, S., Narang, A., and Bhakoo, O.N. Exchange transfusion with G-6-PD deficient donor blood causes exaggeration of neonatal hyperbilirubinemia. Indian Pediatr. 26:499-501, 1989. * Heintz, B., Bock, T.A., Kierdorf, H., and Maurin, N. Haemolytic crisis after acetaminophen in glucose-6-phosphate dehydrogenase deficiency. Klin.Wochenschr. 67:1068, 1989. Notes: Authors claim crisis in patient with Aachen variant of G6PD was due to acetaminophen, although patient had an infection and they state "an infection induced haemolytic crisis cannot.. be ruled out. * Henikoff, S. and Smith, J.M. The human mRNA that provides the N-terminus of chimeric G6PD encodes GMP reductase. Cell 58:1021-1022, 1989. * Hirono, A., Kuhl, W., Gelbart, T., Forman, L., Fairbanks, V.F., and Beutler, E. Identification of the binding domain for NADP+ of human glucose-6-phosphate dehydrogenase by sequence analysis of mutants. Proc.Natl.Acad.Sci.USA 86:10015-10017, 1989. Notes: (B828). * Hirono, A. and Beutler, E. Alternative splicing of human glucose-6-phosphate dehydrogenase mRNA in different tissues. J.Clin.Invest. 83:343-346, 1989. Notes: (B799) MS228. * Jeffery, J., Soderling-Barros, J., Murray, L.A., Wood, I., Hansen, R.J., Szepesi, B., and Jornvall, H. Glucose-6-phosphate dehydrogenase. Characteristics revealed by the rat liver enzyme. Eur.J.Biochem. 186:551-556, 1989. * Jeffery, J., Wood, I., Macleod, A., Jeffery, R., and Jrnvall, H. Glucose-6-phosphate dehydrogenase. Characterization of a reactive lysine residue in the Pichia jadinii enzyme reveals a limited structural variation in a functionally significant segment. Biochem.Biophys.Res.Commun. 160:1290-1295, 1989. * Jonges, G.N., Hagen, H., van Noorden, C.J.F., Weening, R.S., and Roos, D. Comparison between the chromate inhibition test and a cytochemical method for the determination of glucose-6-phosphate dehydrogenase deficiency in erythrocytes. Clin.Chim.Acta 181:135-142, 1989. * Kamchonwongpaisan, S., Bunyaratvej, A., Wanachiwanawin, W., and Yuthavong, Y. Susceptibility to hydrogen peroxide of Plasmodium falciparum infecting glucose-6-phosphate

dehydrogenase-deficient erythrocytes. Parasitology 99:171-174, 1989. * Kanno, H., Huang, I.-Y., Kan, Y.W., and Yoshida, A. Two structural genes on different chromosomes are required for encoding a single chain human red cell glucose-6-phosphate dehydrogenase subunit. Cell 58:595-606, 1989. * Khalifa, A.S., El-Alfy, M.S., Mokhtar, G., Fakeir, A.A., Khazbak, M.A., El-Baz, F., and El-Kholy, M. Effect of desferrioxamine B on hemolysis in glucose-6-phosphate dehydrogenase deficiency. Acta Haematol.(Basel) 82:113-116, 1989. * Koliakos, G., Kalomenopoulou, M., Grammatikos, P., Dimitriadou, A., Kouzi-Koliakos, K., Zacharaki, R., Skaragas, G., Kokka, A., and Trakatellis, A. A new glucose 6-phosphate dehydrogenase variant (G6PD Thessaloniki) in a patient with idiopathic myelofibrosis. Hum.Hered. 39:141-149, 1989. * Lewis, S.M. and Sanders, K.J. Screening for G6PD by Sigma kits. Clin.Lab.Haematol. 11:76-78, 1989. * Luzzatto, L. One enzyme from two genes? Nature 341:286-287, 1989. * Marva, E., Cohen, A., Saltman, P., Chevion, M., and Golenser, J. Deleterious synergistic effects of ascorbate and copper on the development of Plasmodium Falciparum: An in vitro study in normal and in G6PD-deficient erythrocytes. Int.J.Parasitol. 19:779-785, 1989. * Meloni, T., Forteleoni, G., Ogana, A., and Franca, V. Aspirin-induced acute haemolytic anaemia in glucose-6-phosphate dehydrogenase-deficient children with systemic arthritis. Acta Haematol.(Basel) 81:208-209, 1989. * Melzer-Lange, M. and Walsh-Kelly, C. Naphthalene-induced hemolysis in a black female toddler deficient in glucose-6-phosphate dehydrogenase. Pediatr.Emerg.Care 5:24-26, 1989. * Nehal, M. and Baquer, N.Z. Effect of diabetes and insulin-induced hypoglycemia on hexokinase and glucose-6-phosphate dehydrogenase in red blood cells. Biochem.Int. 19:185-191, 1989. * Nehal, M. and Baquer, N.Z. Changes in hexokinase and glucose-6-phosphate dehydrogenase in red cells during hypo and hyper-thyroidism. Biochem.Int. 19:193-199, 1989. * Nero, D., Bowditch, N.,III, Pickert, S., and MacIntyre, R.J. A genetic and molecular analysis of P-induced mutations at the glucose-6-phosphate dehydrogenase locus in Drosophila melanogaster. MGG 219:429-438, 1989. * Owa, J.A. Relationship between exposure to icterogenic agents, glucose-6-phosphate dehydrogenase deficiency and neonatal jaundice in Nigeria. Acta Paediatr.Scand. 78:848-852, 1989. * Pekrun, A., Eber, S.W., and Schrter, W. G6PD Avenches and G6PD Moosburg: biochemical and erythrocyte membrane characterization. Blut 58:11-14, 1989. Notes: Two new G6PD variants with severe enzyme deficiency in Switzerland (G6PD Avenches, G6PD I) and in Germany (G6PD Moosburg, G6PD II) are described. One patient had suffered from severe postpartal hyperbilirubinemia, the other one presented with chronic hemolysis and remittent hyperbilirubinemia. Both variants showed diminished electrophoretic mobility, both variants were heat labile. The Michaelis-Menten constants KM for glucose-6-phosphate and for NADP+ were normal. 2-Desoxy-glucose-6-phosphate was utilized by G6PD I in a higher and by G6PD II at a lower rate than by the normal enzyme. Desamino-NADP+ and galactose-6-phosphate were utilized by both

variants at a normal rate. The electrophoretic separation of membrane proteins of G6PD II showed both in the presence and in the absence of 6-mercaptoethanol no difference concerning the formation of membrane protein aggregates between patient and normal control. * Persico, M.G., Ciccodicola, A., Martini, G., and Rosner, J.L. Functional expression of human glucose-6-phosphate dehydrogenase in Escherichia coli. Gene 78:365-370, 1989. * Rakitzis, E.T. and Papandreou, P.T. Ascorbate-induced generation of free radical species in normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes. Biochem.Soc.Trans. 17:371-372, 1989. * Roth, E.,Jr. and Schulman, S. The parasite derived glucose-6-phosphate dehydrogenase of P. falciparum: What is its role? Prog.Clin.Biol.Res. 313:83-93, 1989. * Schuster, R., Jacobasch, G., and Holzhutter, H.G. Mathematical modelling of metabolic pathways affected by an enzyme deficiency--Energy and redox metabolism of glucose-6-phosphate-dehydrogenase-deficient erythrocytes. Eur.J.Biochem. 182:605-612, 1989. * Serafini, M.T., Romeu, A., and Arola, L. Zn(II), Cd(II) and Cu(II) interactions on glutathione reductase and glucose-6-phosphate dehydrogenase. Biochem.Int. 18:793-802, 1989. Notes: Kinetic characterization of the inhibition effects of Cd(II), Cu(II) and Zn(II) on glutathione reductase (GSSGR; EC 1.6.4.2.) and glucose- 6-phosphate dehydrogenase (G6PD; EC 1.1.1.49) from Saccharomyces cerevisiae was made. No inhibition effect was found with Zn(II) on these enzymatic systems. The effect of Cd(II) (up to 0.16 mM) and Cu(II) (up to 0.008 mM) on GSSGR activity is consistent with a pure competitive inhibition or an uncompetitive pattern, when the varied substrate is the oxidized glutathione or the NADPH, respectively. Only Cd(II) (up to 1.0 mM) showed an inhibition effect on G6PD system, which is consistent with a mixed-type inhibition pattern. When NADP+ changes over an extensive range of concentration, the inhibition effect shows an uncompetitive character. Furthermore, when G-6-P is the varied substrate, the character of the mixed-type inhibition is competitive. * Shantz, L.M., Talalay, P., and Gordon, G.B. Mechanism of inhibition of growth of 3T3-L1 fibroblasts and their differentiatio to adipocytes by dehydroepiandrosterone and related steroids: Role of glucose-6-phosphate dehydrogenase. Proc.Natl.Acad.Sci..USA 86:3852-3856, 1989. * Stamato, T.D., Richardson, E., Ianacone, J., MacLaren, R.A., Denko, N., and Giaccia, A. Isolation and characterization of glucose-6-phosphate dehydrogenase-deficient Chinese hamster cells derived from pure mutant colonies. Mutagenesis 4:259-264, 1989. * van Noorden, C.J.F., Dolbeare, F., and Aten, J. Flow cytofluorometric analysis of enzyme reactions based on quenching of fluorescence by the final reaction product: Detection of glucose-6-phosphate dehydrogenase deficiency in human erythrocytes. J.Histochem.Cytochem. 37:1313-1318, 1989. * Vives-Corrons, J.L., Pujades, A., Petit, J., Colomer, D., Corbella, M., Aguilar i Bascompte, J.L., and Merino, A. Chronic nonspherocytic hemolytic anemia (CNSHA) and glucose 6 phosphate dehydrogenase (G6PD) deficiency in a patient with familial amyloidotic polyneuropathy (FAP). Molecular study of a new variant (G6PD Clinic) with markedly acidic pH optimum. Hum.Genet. 81:161-164, 1989.

* Vulliamy, T.J., Wanachiwanawin, W., Mason, P.J., and Luzzatto, L. G6PD Mahidol, a common deficient variant in South East Asia is caused by a (163)glycine-->serine mutation. Nucleic Acids Res. 17:5868, 1989. * WHO Working Group Glucose-6-phosphate dehydrogenase deficiency. Bull.WHO 67:601-611, 1989. * Yermakov, N.V., Jacobasch, G., Krekhnov, B.V., and Ermakova, T.A. Prognosis of hemolytic anemia in G6PD- subjects. Multifactorial cluster analysis of biochemical characteristics of red cell age groups. Unpublished , 1989. * Yoshida, A. Evolution of glucose-6-phosphate dehydrogenase variants A+ and A-. Blood 74:1860, 1989. * Abdalla, S.H., Phelan, L., and Hussein, H.A. The value of screening tests for glucose-6-phosphate dehydrogenase deficiency. Clin.Lab.Haematol. 12:77-86, 1990. * Aksu, T.A., Esen, F., Dolunay, Aliciguzel, Y., Yucel, G., Cali, S., Baykal, Y. Erythrocyte glucose-6-phosphate dehydrogenase (1.1.1.49) deficiency in Antalya province: an epidemiologic and biochemical study. American Journal of Epidemiology 131(6):1094-1097, 1990. * Argusti, A., Ahluwalia, A., and Mason, P. Personal communication , 1990. * Beutler, E. and Kuhl, W. Linkage between a PvuII restriction fragment length polymorphism and G6PD A-202A/376G: Evidence for a single origin of the common G6PD A- mutation. Hum.Genet. 85:9-11, 1990. Notes: (MS264) (B864). * Beutler, E. and Forman, L. Unpublished , 1990. Notes: G6PD Anaheim; Pt=Wayne Marotte, thrombotic complications Dr. Ken Moser, UCSD & Dr. Otis, Anaheim. * Beutler, E. G-6-PD and galactose phosphate uridyl transferase. In: Handbook of Clinical Chemistry, edited by Werner, M.Florida:CRC Press, 1990, Notes: (MS163) (B883a). * Beutler, E. Glucose-6-phosphate dehydrogenase deficiency. In: Hematology, edited by Williams, W.J., Beutler, E., Erslev, A.J., and Lichtman, M.A.New York:McGraw-Hill, Inc. 1990,p. 591-606. Notes: (B834). * Beutler, E. Genetics of glucose-6-phosphate dehydrogenase deficiency. Semin.Hematol. 27:137-164, 1990. Notes: (B860) (MS257). * Beutler, E., Lisker, R., and Kuhl, W. Molecular biology of G6PD variants. Biomed.Biochim.Acta 49:236-241, 1990. Notes: (B824) (MS265). * Beutler, E., Forman, L., Gelbart, T., and Means, R.T. Unpublished , 1990. Notes: G6PD Nashville. Patient=Wallace Carter; Physician=Robert T. Means, VA Medical Center, Nashville. * Beutler, E., Gelbart, T., and Kuhl, W. Human red cell glucose-6-phosphate dehydrogenase: All active enzyme has sequence predicted by the X-chromosome encoded cDNA. Cell 62:7-9, 1990. Notes: (MS280) (B881). * Beutler, E. and Kuhl, W. The NT 1311 polymorphism of G6PD: G6PD Mediterranean mutation may have originated independently in Europe and Asia. Am.J.Hum.Genet. 47:1008-1012, 1990. Notes: (MS282) (B880). * Bhatia, R.P.S., Patel, R., and Dubey, B. Senile cataract and glucose-6-phosphate dehydrogenase deficiency in Indians. Trop.Geogr.Med. 42:349-351, 1990. * Brabin, L. and Brabin, B.J. Malaria and glucose 6-phosphate

dehydrogenase deficiency in populations with high and low spleen rates in Madang, Papua New Guinea. Hum.Hered. 40:15-21, 1990. * Calabro, V., Giacobbe, A., Vallone, D., Montanaro, V., Cascone, A., Filosa, S., and Battistuzzi, G. Genetic heterogeneity at the glucose-6-phosphate dehydrogenase locus in southern Italy: A study on a population from the Matera district. Hum.Genet. 86:49-53, 1990. Notes: Glucose-6-phosphate dehydrogenase (G6PD) has been analyzed by gel electrophoresis and by quantitative assay in an unselected sample of 1524 schoolboys from the province of Matera (Lucania) in southern Italy. We have identified 43 subjects with a G6PD variant. Of these, 31 had severe G6PD deficiency, nine had mild to moderate deficiency, and three had a non- deficient electrophoretic variant. The overall rate of G6PD deficiency was 2.6%. The frequency of G6PD deficiency, ranging from 7.2% on the Ionian Coast to zero on the eastern side of the Lucanian Apennines, appears to be inversely related to the distance of each town examined from the Ionian Coast, suggesting that this geographic distribution may reflect, at least in part, gene flow from Greek settlers. Biochemical characterization has shown that most of the G6PD deficiency in this population is accounted for by G6PD Mediterranean. In addition, we have found several examples of two other known polymorphic variants (G6PD Cagliari and G6PD A-); th * Cho, S.-W. and Joshi, J.G. Characterization of glucose-6-phosphate dehydrogenase isozymes from human and pig brain. Neuroscience 38:819-828, 1990. Notes: Homogenates of human and pig brain in 10 mM Tris-HCl, pH 8.0 were centrifuged at 25,400 x g for 1 h. The supernatants were electrophoresed in polyacrylamide gels and the gels were stained for glucose-6-phosphate dehydrogenase (EC 1.1.1.49) activity. Five distinct bands were visible. Isozymes corresponding to two of those bands were purified from human and pig brain. The isozymes were electrophoretically homogeneous. The native proteins, Mr, 220,000, dissociated in sodium dodecyl sulphatepolyacrylamide gels into a 57,000 Mr subunit. Therefore, the native isozymes are tetramers. None of the isozymes required additional metal ions for activity. At 1 mM concentration Mg2+ and Ca2+, independently or together, activated the isozymes 1.5-fold. The isozymes were NADP+- specific. Kmapp values of the G6PD isozymes were similar for NADP+ (6-8 uM), but different for G6P (56-180 uM). The specific activities of the isozymes varied from 50 to 210 units per mg of protein. All isozymes were inhibited by NADPH. The * Crans, D.C. and Schelble, S.M. Vanadate dimer and tetramer both inhibit glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. Biochemistry 29:6698-6706, 1990. Notes: Vanadate dimer and tetramer inhibit glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. The inhibition by a vanadate mixture containing vanadate monomer, dimer, tetramer, and pentamer was determined by measuring the rates of glucose 6-phosphate oxidation and reduction of NAD (or NADP) catalyzed by glucose-6-phosphate dehydrogenase. The inhibition by vanadate is competitive with respect to NAD or NADP and noncompetitive (a mixed type) with respect to glucose 6- phosphate (G6P) when NAD or NADP are cofactors. This inhibition pattern varies from that observed with phosphate and thus suggests vanadate interacts differently than a phosphate analogue with the enzyme. 51V NMR spectroscopy was used to directly correlate the inhibition of vanadate solutions to the vanadate dimer and/or tetramer,

respectively. The activity of the vanadate oligomer varied depending on the cofactor and which substrate was being varied. The vanadate dimer was the major inhibiting species with respect to NADP. This * D'Urso, M., Zucchi, I., Ciccodicola, A., Palmieri, G., Abidi, F.E., and Schlessinger, D. Human glucose-6-phosphate dehydrogenase gene carried on a yeast artificial chromosome encodes active enzyme in monkey cells. Genomics 7:531-534, 1990. * De, O.B. and Nonoyama, K. GB(-) Carapicuiba, a new rare glucose-6-phosphate dehydrogenase variant with moderate deficiency presenting chronic non spherocytic hemolytic anemia. Blood 76(Suppl):30a, 1990. * Delgado, C., Tejedor, M.C., and Luque, J. Partial purification of glucose 6-phosphate dehydrogenase and phosphofructokinase from rat erythrocyte haemolysate by partitioning in aqueous two-phase systems. J.Chromatogr. 498:159-168, 1990. * Dess , S., Batetta, B., Pani, P., Barra, S., Miranda, F., and Puxeddu, P. Glucose-6-phosphate dehydrogenase (G6PD) activity in tumoral tissues of G6PD-deficient subjects affected by larynx carcinoma. Cancer Lett. 53:159-162, 1990. Notes: The activity of glucose-6-phosphate dehydrogenase (G6PD), the key enzyme of the hexose monophosphate (HMP) shunt pathway, was measured in both normal and tumoral larynx tissues from normal and G6PD deficient subjects. Significant increases of this enzymatic activity were found in tumoral tissues of both normal and G6PD deficient subjects, who were characterized by very low levels of G6PD activity in erythrocytes as well as in larynx tissue. AUTHOR. * Dutta, P., Rivlin, R.S., and Pinto, J. Enhanced depletion of lens reduced glutathione by Adriamycin in riboflavin-deficient rats. Biochem.Pharmacol. 40:1111-1115, 1990. Notes: The anticancer drug Adriamycin (registered) has photosensitizing properties which potentially may be detrimental to lens tissue. Since reduced glutathione (GSH) serves to protect lens from photo-oxidative stress and dietary riboflavin is required by glutathione reductase to regenerate GSH, we investigated whether Adriamycin (registered) intensifies the depletion of GSH levels in rat lens during dietary riboflavin deficiency. Three-week- old rats were divided into two groups. One group was fed a diet deficient in riboflavin (<1 ppm) and the other group was pair-fed a control diet containing adequate riboflavin (8.5 ppm). After 6-12 weeks of dietary treatment, half the animals in each dietary group received Adriamycin (registered) (8 mg/kg/day) intraperitoneally for 3 days. After killing the rats, lenses were removed, and GSH content and glutathione reductase activity were measured in freshly prepared homogenates. To determine the extent of systemic oxidative stress and the degree of riboflavin defici * Egli, F.L., Koller, B., and Furrer, J. Hairy-cell leukemia and glucose-6-phosphate dehydrogenase deficiency in two brothers. N.Engl.J.Med. 322:1159, 1990. * El-Hazmi, M.A.F. and Warsy, A.S. Frequency of glucose-6-phosphate dehydrogenase variants and deficiency in Arabia. Gene Geography 4:15-20, 1990. * El-Hazmi, M.A.F., Al-Swailem, A.R., Bahakim, H.M., Al-Faleh, F.Z., and Warsy, A.S. Effect of alpha thalassaemia, G-6-PD deficiency and Hb F on the nature of sickle cell anaemia in south-western Saudi Arabia. Trop.Geogr.Med. 42:241-247, 1990.

* Fey, M.F., Wainscoat, J.S., Mukwala, E.C., Falusi, A.G., Vulliamy, T.J., and Luzzatto, L. A PvuII restriction fragment length polymorphism of the glucose-6-phosphate dehydrogenase gene is an African-specific marker. Hum.Genet. 84:471-472, 1990. Notes: The site of a PvuII restriction fragment length polymorphism (RFLP) of the human glucose-6-phosphate dehydrogenase (G6PD) gene has been located in intron V, 60bp upstream of G6PD exon VI. A population survey shows this RFLP to be specific for African populations, with frequencies of the rarer allele (PvuII type 2 site present) of 0.32-0.40 in Kenyans, Nigerians, Zambians, and West Indians. This allele has not been found in the European, Asian and Middle Eastern populations studied. Such population-specific markers may be useful in the study of population affinities and may provide insight into prehistoric migrations of peoples. AUTHOR. * Fiorelli, G., Meloni, T., Palomba, V., Manoussakis, C., Villa, S., and Cappellini, M.D. Gene frequency of glucose-6-phosphate dehydrogenase (G6PD) polymorphic variants in Sardinia. Gene Geography 4:139-142, 1990. * Fiorelli, G., Anghinelli, L., Carandina, G., Toniolo, D., Sempietro, M., Cappellini, M.D., and Pareti, F.I. Point mutations in two G6PD variants previously described in Italy. Blood 76(Suppl):7a, 1990. * Fujii, H. and Miwa, S. Recent progress in the molecular genetic analysis of erythroenzymopathy. Am.J.Hematol. 34:301-310, 1990. Notes: During the relatively recent period in which normal genes for most red cell enzymes have been isolated, the techniques of molecular biology have been applied to the studies of erythroenzymopathy. Single nucleotide substitutions have been identified in aldolase, triosephosphate isomerase, glucose 6-phosphate dehydrogenase, and adenylate kinase variants by the cloning and nucleotide sequence of the patients' genes. Up to now, all of the enzyme-deficient variants which have been investigated have been caused by point mutations. An exception is a hemolytic anemia secondary to increased adenosine deaminase (ADA) activity. Red cell ADA activity increases on the order of a hundred-fold in affected individuals. The basic abnormality appears to result from overproduction of structurally normal enzyme due to abnormal transcriptional or translational efficiency. AUTHOR. * Gaetani, G.F., Galiano, S., Melani, C., Miglino, M., Forni, G.L., Napoli, G., Perrone, L., and Ferraris, A.M. A new glucose-6-phosphate dehydrogenase variant with congenital nonspherocytic hemolytic anemia (G6PD Genova). Biochemical characterization and mosaicism expression in the heterozygote. Hum.Genet. 84:337-340, 1990. Notes: A new deficient variant of glucose-6-phosphate dehydrogenase (G6PD) causing severe congenital nonspherocytic hemolytic anemia (CNSHA) is described. The variant enzyme, characterized by slow electrophoretic mobility, extreme in vivo and in vitro lability, high Km for G6P and strongly acidic pH optimum, appears to be unique, and has been designated G6PD Genova. Investigation of an obligate heterozygote using various cytochemical, biochemical and recombinant-DNA techniques showed G6PD mosaicism in the erythrocytes and leukocytes. Therefore, the presence of a disadvantageous mutation at one Gd locus did not determine selection in favor of the normal allele in the heterozygote's hemopoietic cells. AUTHOR. * Glatz, Z., Tomandl, J., Janiczek, O., and Marek, A.

Chromatographic purification of glucose-6-phosphate dehydrogenase and lactate dehydrogenase from Leuconostoc mesenteroides. J.Chromatogr. 503:197-204, 1990. Notes: A simple procedure for the simultaneous purification of glucose-6- phosphate dehydrogenase and lactate dehydrogenase from Leuconostoc mesenteroides is described. It involves ammonium sulphate precipitation, hydrophobic interaction chromatography and ion-exchange chroamtography. The purity of the final fractions is checked by size-exclusion chromatography and by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate. The purified enzymes are suitable for enzymological studies and analytical biochemistry. AUTHOR. * Goldman, F., Rotbart, H., Gutierrez, K., and Ambruso, D. Parvovirus-associated aplastic crisis in a patient with red blood cell glucose-6-phosphate dehydrogenase deficiency. Pediatr.Infect.Dis.J. 9:593-594, 1990. * Gonzalez, O.L., Espina, A., and Calcines, P. G6P-DH Santa Clara and G6P-DH Villa Clara: two new Cuban variants. Acta Paediatr.Hung. 30:17-26, 1990. * Jacobasch, G., Sakalova, A., and Brabeck, V. Heterogeneity of glucose-6-phosphate dehydrogenase enzymopathies in the CSSR. Biomed.Biochim.Acta 49:S247-S250, 1990. * Jorgensen, A.L., Deeb, S.S., and Motulsky, A.G. Molecular genetics of X chromosome-linked color vision among populations of African and Japanese ancestry: High frequency of a shortened red pigment gene among Afro-Americans. Proc.Natl.Acad.Sci.USA 87:6512-6516, 1990. * Karunanithy, R., Saha, N., and Ng, S.E. Serum and red blood cell magnesium, copper, and zinc content in G6PD deficiency. Am.J.Hematol. 35:136-138, 1990. * Kemper, C.A., Tucker, R.M., Lang, O.S., Kessinger, J.M., Greene, S.I., Deresinski, S.C., and Stevens, D.A. Low-dose dapsone prophylaxis of Pneumocystis carinii pneumonia in AIDS and AIDS-related complex. AIDS 4:1145-1148, 1990. * Kilin , Y. and Kumi, M. Haemolytic crises due to glucose-6-phosphate dehydrogenase deficiency in the mid-southern region of Turkey. Acta Paediatr.Scand. 79:1075-1079, 1990. Notes: Clinical and laboratory evaluation of 60 boys with hemizygous, 12 girls with homozygous, and 11 girls with heterozygous erythrocyte glucose-6- phosphate dehydrogenase deficiency was made during haemolytic crisis. The main clinical symptoms were paleness, dark urine and oliguria. Only one patient needed peritoneal dialysis. Coexistence of glucose-6-phosphate dehydrogenase deficiency associated with haemoglobinopathy was found to be higher than expected (32 out of 83 cases). Also, the high prevalence of glucose-6-phosphate dehydrogenase deficiency among females with homozygous and heterozygous disease was surprising. The precipitating factors of haemolysis were variable. Rather than antimalarial and antipyretic-analgesic drugs, infections seemed to he the main haemolytic factor. Key words: ,glucose-6-phosphate dehydrogenase deficienA, haemoglobinopathy. AUTHOR. * Kurdi-Haidar, B. and Luzzatto, L. Expression and characterization of glucose-6-phosphate dehydrogenase of Plasmodium falciparum. Mol.Biochem.Parasitol. 41:83-92, 1990. Notes: Glucose-6-phosphate dehydrogenase (G6PD) from Plasmodium falciparum has been detected previously in cultures of parasites grown in G6PD- deficient red blood cells. Using polyacrylamide gel electrophoresis, a semi- quantitative assay has been developed to compare the level of the parasite enzyme activity

in G6PD normal and in G6PD-deficient host cells. The results do not support the previous contention that the host cell G6PDdeficiency necessarily affects the level of expression of the parasite enzyme. The plasmodial enzyme was partially purified from extracts of parasites prepared by digitonin lysis of infected red blood cells, and its distinctive biochemical properties are described. P. falciparum G6PD has a K(G6P/m) of 27 uM, a K(NADP/m) of 4.5 uM, and K(NADPH/i) of 4.5 uM, indicating an affinity for all its main ligands much higher than that of normal human red cell G6PD. AUTHOR. * Kurdi-Haidar, B., Mason, P.J., Berrebi, A., Ankra-Badu, G., Al-Ali, A., Oppenheim, A., and Luzzatto, L. Origin and spread of the glucose-6-phosphate dehydrogenase variant (G6PD-Mediterranean) in the Middle East. Am.J.Hum.Genet. 47:1013-1019, 1990. Notes: A common glucose-6-phosphate dehydrogenase (G6PD) variant characterized by severe enzyme deficiency and B-like electrophoretic mobility is called "G6PD-Mediterranean" because it is found in different populations around the Mediterranean Sea. Sequence analysis of Italian subjects has revealed that the molecular basis of G6PD-Mediterranean is a single C-T transition at nucleotide position 563, causing a serine phenylalanine replacement at amino acid position 188. Most G6PD-Mediterranean subjects also have a silent C-T transition (without amino acid replacement) at nucleotide position 1311. Twenty-one unrelated individuals from Saudi Arabia, Iraq, Iran, Jordan, Lebanon, and Israel with both severe G6PD deficiency and B- like electrophoretic mobility were tested for both mutations by using amplification followed by digestion with appropriate restriction enzymes. All but one had the 563 mutation, and, of these, all but one had the 1311 mutation. Another 24 unrelated Middle Eastern individuals with normal * Luckinbill, L.S., Riha, V., Rhine, S., and Grudzien, T.A. The role of glucose-6-phosphate dehydrogenase in the evolution of longevity in Drosophila melanogaster. Heredity 65:29-38, 1990. * Luzzatto, L. and Mehta, A. Glucose 6-phosphate dehydrogenase deficiency. In: The Metabolic Basis of Inherited Disease, edited by Scriver, C.R., Beaudet, A.L., Sly, W.S., and Valle, D.New York:McGraw-Hill Information Services Co. 1990,p. 2237-2265. * Mason, P.J., Bautista, J.M., Vulliamy, T.J., Turner, N., and Luzzatto, L. Human red cell glucose-6-phosphate dehydrogenase is encoded only on the X chromosome. Cell 62:9-10, 1990. * Mehta, J.B., Singhal, S.B., and Mehta, B.C. Ascorbic-acid-induced haemolysis in G-6-PD deficiency. Lancet 336:944, 1990. * Meloni, T., Carta, F., Forteleoni, G., Carta, A., Ena, F., and Meloni, G.F. Glucose 6-phosphate dehydrogenase deficiency and cataract of patients in Northern Sardinia. Am.J.Ophthalmol. 110:661-664, 1990. Notes: We determined the activity level of glucose 6-phosphate dehydrogenase in 467 patients with cataract from northern Sardinia. Of 226 men, 18 (8%) had glucose 6-phosphate dehydrogenase deficiency. Of 241 women, 30 (12%) were heterozygous and two (1%) were homozygous for glucose 6-phosphate dehydrogenase deficiency. These prevalences were not significantly different from those expected in the general population. We concluded that patients with glucose 6-phosphate dehydrogenase deficiency do not have a higher risk of developing cataract. AUTHOR.

* Mosca, A., Marialaura, P., Sanna, A., Paleari, R., Cao, A., and Galanello, R. Preliminary experience with the differential pH technique for glucose-6-phosphate dehydrogenase (G6PD) measurement in whole blood: Application to an area with high prevalance of thalassaemia and G6PD deficiency. Haematologica (Pavia) 75:397-399, 1990. * Muller, A. and Somoza, R. Glycolytic, glucose-6-phosphate dehydrogenase and related erythroenzymopathies in Venezuelan patients with congenital hemolytic anemia or cyanosis. Blood 76(Suppl):42a, 1990. * Nagel, R.L. Innate resistance to malaria: the intraerythrocytic cycle. Blood Cells 16:321-339, 1990. Notes: The human innate resistance to P. falciparum malaria is based on genetic features that affect several stages of the intraerythrocytic cycle of the plasmodia. HbS, HbE and alpha and beta thalassemia (in addition to G-6PD deficiency) are protective to the carriers, because they inhibit the intraerythrocytic growth period, and in the case of AS red cells, in addition, parasitosis make them detectable expeditiously by the spleen. Blood group polymorphisms can interfere with red cell invasion by plasmodia. HbC belongs to a special category, since it apparently interferes with the cycle at the moment of cell lysis and release of merozoites. Finally, ovalocytosis observed in South East Asia, which most likely corresponds to a cytoskeleton or membrane protein defect, protects from malaria by inhibiting invasion. It should be kept in mind that many of these red cell defects might protect individuals in the critical first 5 years of life by retarding the switch of HbF to adult hemoglobin, since the HbF contai * Nehal, M., Azam, M., and Baquer, N.Z. Changes in the levels of catecholamines, hexokinase and glucose 6-phosphate dehydrogenase in red cell aging. Biochem.Int. 22:517-522, 1990. Notes: The activity of the enzymes hexokinase and glucose 6-phosphate dehydrogenase and the level of catecholamines were measured in isolated rat Red Blood Cells (RBC) during cellular aging. The results clearly showed a linear decline in the two enzyme profile with corresponding increase in age of RBC. A decrease of 75-85% in the activities were found in the oldest cell fractions as compared to the youngest. The levels of glycosylated haemoglobin and catecholamines were found to increase with aging. A correlation can probably be established between the enzyme activities, the levels of glycosylated haemoglobulin and catecholamines during aging. AUTHOR. * Niazi, G.A., Drouin, D.J., and Hawa, L.A. Erythrocytic glucose-6-phosphate dehydrogenase deficiency and anaemia. Saudi Med.J. 11:221-223, 1990. * Niazi, G.A., Yaish, H.M., Dery, J.P., and Al Shaalan, M. Erythrocytic genetic disorders in the newborn population of Saudi Arabian National Guard. Saudi Med.J. 11:497-500, 1990. * Ninfali, P., Orsenigo, I., Baronciani, L., and Rapa, S. Rapid purification of glucose-6-phosphate dehydrogenase from mammal's erythrocytes. Prep.Biochem. 20:297-309, 1990. * Nogae, I. and Johnston, M. Isolation and characterization of the ZWF1 gene of Saccharomyces cerevisiae, encoding glucose-6-phosphate dehydrogenase. Gene 96:161-169, 1990. Notes: Glucose-6-phosphate dehydrogenase (G6PD) catalyzes the first step of the pentose phosphate pathway, a reaction that generates NADPH. We have isolated ZWF1, the Saccharomyces cerevisiae gene that encodes G6PD, and identified its transcript and transcription start point. Expression of ZWF1 appears not to

be regulated, consistent with its 'housekeeping' role. Null mutants lacking G6PD appear to grow normally, but are more sensitive than wild type to oxidizing agents that presumably reduce the level of NADPH. This suggests that G6PD has a major role in NADPH production in yeast. Regulation of GAL1 expression appears normal in zwf1 mutants, suggesting that the pentose phosphate pathway is not involved in glucose repression. The predicted amino acid sequence of yeast G6PD is highly similar to the sequence of the Drosophila, human, and rat enzymes, except near its N terminus, where the yeast and Drosophila sequences diverge from that of human and rat. AUTHOR. * Nwankwo, M.U., Bunker, C.H., Ukoli, F.A., Omene, J.A., Freeman, D.T., Vergis, E.N., Yeh, L.L., and Kuller, L.H. Blood pressure and other cardiovascular disease risk factors in black adults with sickle cell trait or glucose-6-phosphate dehydrogenase deficiency. Genet.Epidemiol. 7:211-218, 1990. * rstan, A. and Gafni, A. Enhanced proteolysis of glucose-6-phosphate dehydrogenase in the presence of palmitoyl coenzyme A. Biochem.Int. 21:915-921, 1990. Notes: Palmitoyl coenzyme A at concentrations below its critical micelle concentration increases the rate of proteolysis of baker's yeast glucose-6- phosphate dehydrogenase by proteinase A in the pH range 4-5. Both glucose- 6-phosphate and NADP protect glucose-6-phosphate dehydrogenase against proteolysis, but these protective effects are diminished in the presence of palmitoyl coenzyme A. Since palmitoyl coenzyme A is known to dissociate glucose-6-phosphate dehydrogenase into dimers, the results imply that the in vivo half life of glucose-6-phosphate dehydrogenase may be controlled by a process based on the regulation of the oligomeric structure of the enzyme by the collective actions of various molecules, including palmitoyl coenzyme A. AUTHOR. * Paleari, R., Ceriotti, F., Bonini, P.A., and Mosca, A. Standardization problems relevant to quantitative laboratory methods for glucose-6-phosphate dehydrogenase deficiency detection. Giorn.It.Chim.Clin. 15:191-198, 1990. * Papandreou, P.T. and Rakitzis, E.T. Inhibition by a free-radical scavenger of ascorbate-induced hemoglobin denaturation in glucose-6-phosphate dehydrogenase deficient erythrocytes. Clin.Chim.Acta 189:253-254, 1990. * Poggi, V., Town, M., Foulkes, N.S., and Luzzatto, L. Identification of a single base change in a new human mutant glucose-6-phosphate dehydrogenase gene by polymerase-chain-reaction amplification of the entire coding region from genomic DNA. Biochem..J. 271:157-160, 1990. Notes: We report the characterization at the molecular level of a mutant glucose- 6-phosphate dehydrogenase (G6PD) gene in a Greek boy who presented with a chronic nonspherocytic haemolytic anaemia. In order to identify the mutation from a small amount of patient material, we adopted an approach which by-passes the need to construct a library by using the polymerase chain reaction. The entire coding region was amplified in eight sections, with genomic DNA as template. The DNA fragments were then cloned in an M 13 vector and sequenced. The only difference from the sequence of normal G6PD was a T-->G substitution at nucleotide position 648 in exon 7, which predicts a substitution of leucine for phenylalanine at amino acid position 216. This mutation creates a new recognition site for the restriction nuclease BalI. We confirmed the presence of the mutation in the DNA of the patient's mother, who was found to be heterozygous for the new BalI site. This is the first transversion among the point

mutations thus f * Rakitzis, E.T., Manolakou, K., and Papandreou, P. Spectrophotometric evaluation of results of the ascorbate and the ascorbate-cyanide screening tests for glucose-6-phosphate dehydrogenase deficiency. Clin.Chim.Acta 187:189-192, 1990. * Scott, M.D., Zuo, L., Lubin, B.H., and Chiu, D.T.Y. NADPH status, not glutathione, modulates hemoglobin oxidant susceptibility in normal and glucose-6-phosphate dehydrogenase deficient red cells. Blood 76:17a, 1990. * Sheriff, D.S. and El Fakhri, M. Serum lipoprotein profile and concentration of dehydroepiandrosterone sulfate (DHEAS) in glucose-6-phosphate dehydrogenase-deficient subjects. Clin.Chem. 36:393-394, 1990. * Stevens, D.J., Wanachiwanawin, W., Mason, P.J., Vulliamy, T.J., and Luzzatto, L. G6PD Canton a common deficient variant in South East Asia caused by a 459 Arg-->Leu mutation. Nucleic Acids Res. 18:7190, 1990. * Town, M., Athanasiou-Metaxa, M., and Luzzatto, L. Intragenic interspecific complementation of glucose-6-phosphate dehydrogenase in human-hamster cell hybrids. Somat.Cell Mol.Genet. 16:97-108, 1990. * Ursini, M.V., Scalera, L., and Martini, G. High levels of transcription driven by a 400 bp segment of the human G6PD promoter. Biochem.Biophys.Res.Commun. 170:1203-1209, 1990. Notes: A 2850-base-pair-long DNA segment containing the transcriptional start site of the human X-linked gene coding for the housekeeping enzyme glucose-6-phosphate dehydrogenase has been fused to the reporter chloramphenicol acetyl transferase gene. This fusion was introduced into three different mammalian cell lines (HepG2, CVI and HeLa).Strong expression was detected and transcription initiated at the natural start site. By deletion analysis, we determined that a 436 base pair region of this promoter is sufficient for full expression of the chimaeric construct and therefore the remainder of the CpC island surrounding the transcriptional start site and differentially methylated in the active and inactive X chromosome is not necessary for transcriptional activity in this assay. Further sequence deletions from -436 to -116 base pairs decrease the promoter-directed chloramphenicol acetyl transferase activity. Site- directed mutagenesis of a TATA-like sequence present in the G6PD promoter shows that this sit * Viglietto, G., Montanaro, V., Calabro, V., Vallone, D., D'Urso, M., Persico, M.G., and Battistuzzi, G. Common glucose-6-phosphate dehydrogenase (G6PD) variants from the Italian population: Biochemical and molecular characterization. Ann.Hum.Genet. 54:1-15, 1990. * Vives-Corrons, J.-L., Kuhl, W., Pujades, M.A., and Beutler, E. Molecular genetics of G6PD Mediterranean variant and description of a new G6PD mutant, G6PD Andalus1361A. Am.J.Hum.Genet. 47:575-579, 1990. Notes: (MS276) (B869). * Yoshida, A. and Kan, Y.W. Origin of "fused" glucose-6-phosphate dehydrogenase. Cell 62:11-12, 1990. * Zuo, L., Chen, E., Du, C.S., Chang, C.N., and Chiu, D.T.Y. Genetic study of Chinese G6PD variants by direct PCR sequencing. Blood 76 (Suppl):51a, 1990. * Adediran, S.A. Kinetic properties of normal human erythrocyte glucose-6-phosphate dehydrogenase dimers. Biochim.Biophys.Acta 73:1211-1218, 1991. Notes: The steady-state kinetics of normal human erythrocyte

glucose- 6-phosphate dehydrogenase (D-glucose-6-phosphate: NADP+ oxidoreductase, EC 1.1.1.49) dimers were studied as a function of pH and temperature. Inhibition studies using glucosamine 6-phosphate, NADPH and p- hydroxymercuribenzoate (P-OHMB) were also carried out at pH 8.0. The existence of two binding sites on the enzyme with a transition from low to high affinity for NADP+ when NADP+ concentration is increased is indicated by the nonlinear Lineweaver-Burk plots and sigmoid kinetic patterns. NADPH inhibition was found to be competitive with respect to NADP+ and non- competitive with respect to glucose- 6-phosphate. Logarithmic plot of Vmax against pH and inactivation by P-OHMB indicate the participation in the reaction mechanism of imidazolium group of histidine and sulfydryl groups. The initial velocity and product inhibition data gave results which are consistent with the dimeric enzyme following an ordered sequential mechanism. A possible * Beutler, E., Gilsanz, F., and Toscano, R.M. More on the association of glucose-6-phosphate dehydrogenase deficiency with hairy-cell leukemia. N.Engl.J.Med. 324:1370, 1991. Notes: (MS298) (B889). * Beutler, E. Glucose-6-phosphate dehydrogenase (G6PD) deficiency. N.Engl.J.Med. 324:169-174, 1991. Notes: (MS294) (B884). * Beutler, E., Kuhl, W., Ramirez, E., and Lisker, R. Some Mexican glucose-6-phosphate dehydrogenase (G-6-PD) variants revisited. Hum.Genet. 86:371-374, 1991. Notes: (MS288) (B890). * Beutler, E. Hemolysis from exposure to naphthalene mothballs. Reply. N.Engl.J.Med. 325:1660-1661, 1991. Notes: (MS329) (B905a). * Beutler, E., Kuhl, W., Gelbart, T., and Forman, L. DNA sequence abnormalities of human glucose-6-phosphate dehydrogenase variants. J.Biol.Chem. 266:4145-4150, 1991. Notes: (MS290) (B888). * Beutler, E., Prchal, J.T., Westwood, B., and Kuhl, W. Definition of the mutations of G6PD Wayne, G6PD Viangchan, G6PD Jammu and G6PD "LeJeune". Acta Haematol.(Basel) 86:179-182, 1991. Notes: (MS313)(B919). * Beutler, E. Glucose-6-phosphate dehydrogenase deficiency. Reply. N.Engl.J.Med. 324:1743, 1991. Notes: (B892). * Beutler, E., Kuhl, W., S enz, G.F., and Rodriguez, W. Mutation analysis of G6PD variants in Costa Rica. Hum.Genet. 87:462-464, 1991. Notes: (MS302) (B901). * Canepa, L., Ferraris, A.M., Miglino, M., and Gaetani, G.F. Bound and unbound pyridine dinucleotides in normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes. Biochim.Biophys.Acta 1074:101-104, 1991. Notes: We have measured, by a sensitive cycling assay, the concentration of bound and unbound dinucleotides in normal and glucose-6-phosphate dehydrogenase (G6PD)-deficient erytbrocytes. Measurement of free NADP in ultrafiltrates confirms that in normal erythrocytes almost all NADP is bound to cytosolic proteins. In glucose-6-phosphate dehydrogenase-deficient erythrocytes unbound NADP is significantly higher than in normal red cells and the NADP+/NADPH ratio is largely in favor of the oxidized form. In normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes essentially all NAD (bound and unbound) is in the oxidized state. About 50% of the total

amount of NAD (NAD+ + NADH) is free in the cytosol, with a NAD+/NADH ratio greater than 100. AUTHOR.. * Chao, L., Du, C.-S., Louie, E., Zuo, L., Chen, E., Lubin, B., and Chiu, D.T.Y. A to G substitution identified in exon 2 of the G6PD gene among G6PD deficient Chinese. Nucleic Acids Res. 19:6056, 1991. * Chen, E.Y., Cheng, A., Lee, A., Kuang, W.-J., Hillier, L., Green, P., Schlessinger, D., Ciccodicola, A., and D'Urso, M. Sequence of human glucose-6-phosphate dehydrogenase cloned in plasmids and a yeast artificial chromosome (YAC). Genomics 10:792-800, 1991. * Chiu, D.T.Y., Zuo, L., Chen, E., Chao, L.T., Louie, E., Lubin, B.H., and Du, C.S. DNA sequence abnormalities in Chinese glucose-6-phosphate dehydrogenase (G6PD) variants. Blood 78:252a, 1991. * Chiu, D.T.Y., Zuo, L., Chen, E., Chao, L., Louie, E., Lubin, B., Liu, T.Z., and Du, C.-S. Two commonly occurring nucleotide base substitutions in Chinese G6PD variants. Biochem.Biophys.Res.Commun. 180:988-993, 1991. Notes: Using a direct PCR sequencing technique, we have identified two DNA base substitutions in 8 different biochemical G6PD variants of Chinese origin. Neither one of these abnormalities has been reported in other ethnic groups. An abnormality (C1) of G toT substitution at cDNA 1376 causing an amino acid change from Arg to Leu has been found in 3 variants. Another abnormality (C2) of G to A substitution at cDNA 1388 causing an amino acid change from Arg to His has been found in 5 variants. Both C1 and C2 are located in exon 12 of the G6PD gene and are only 12 base pairs apart. However, C1 is associated with a significant increase in the deamino- NADP utilization rate, whereas C2 is not. Taken together, our data suggest that C1 and C2 are very common among Chinese with a G6PD deficiency and exon 12 may define an important functional domain of the human G6PD. Copyright 1991 Academic Press, Inc. * Cox, G. and Roberts, M.S. Glucose-6-phosphate dehydrogenase deficiency. N.Engl.J.Med. 324:1742-1743, 1991. * Ducros, J., Saingra, S., Rampal, M., Coulange, C., Barbe, M.-C., and Verzetti, G. Hemolytic anemia due to G6PD deficiency and urate oxidase in a kidney-transplant patient. Clin.Nephrol. 35:89-90, 1991. * El-Hazmi, M.A.F., Jabbar, F.A., Al-Faleh, F.Z., Al-Swailem, A.R., and Warsy, A.S. Patterns of sickle cell, thalassaemia and glucose-6-phosphate dehydrogenase deficiency genes in north-western Saudi Arabia. Hum.Hered. 41:26-34, 1991. * El-Hazmi, M.A.F. and Warsy, A.S. Glucose-6-phosphate dehydrogenase variants and sickle cell genes in Al-Qunfuda, Saudi Arabia. Trop.Geogr.Med. 43:174-179, 1991. * Filippi, G., Arslanian, A., Dagna-Bricarelli, F., Pierluigi, M., Grasso, M., Rinaldi, A., Rocchi, M., and Siniscalco, M. Premutation for the Martin-Bell syndrome analyzed in a large pedigree segregating also for G6PD-deficiency. I: A working hypothesis on the nature of the FRAX-mutations. Am.J.Med.Genet. 40:387-394, 1991. Notes: A large Sardinian family including 13 Martin-Bell syndrome (MBS) patients, several instances of normal transmitting males or females, and the G6PD- Mediterranean mutant segregating in some of its branches, has been thoroughly investigated with the hope of gaining further insight on the nature of the FRAX-mutation. All the MBS patients and the 15 obligate heterozygous women present in the pedigree could be traced back

through their X-chromosome lineage to the same ancestress, who must have been heterosygous for a silent premutation at the FRAX-locus. This premutation appears to have turned into a true FRAX-mutation at least 9 times during the gametogenesis of the ancestress' X-related descendants of whom four are males. This finding alone suggests that the transition from the FRAX premutation to the true mutation can be the result of intra- as well as interchromosomal events. This conclusion is supported by the additional observation that the genetic phase between the FRAX and the G6PD loci remained * Forbes, J., Steytler, J.G., and Van Heerden, R. Agarose gel electrophoresis of glucose-6-phosphate-dehydrogenase isoenzymes. Clin.Chim.Acta 199:279-282, 1991. * Horn, S., Bashan, N., and Gopas, J. Phagocytosis of phenylhydrazine oxidized and G-6-PD-deficient red blood cells: The role of cell-bound immunoglobulins. Blood 78:1818-1825, 1991. Notes: In this study, the role of Igs in the recognition and removal of oxidatively damaged human red blood cells (RBCs) was investigated. Phagocytosis of normal RBCs exposed to the oxidative hemolytic agent phenylhydrazine (Phz) and of glucose6-phosphate dehydrogenase (G6PD)-deficient RBCs by murine macrophages was examined. A 40-fold increase in phagocytosis of RBCs treated with 3 mmol/L Phz was obtained both in the absence and presence of autologous serum, indicating that binding of autologous antibodies to the oxidized cells is not essential for phagocytosis. Yet, a basal number of IgG molecules was found to be present on the RBCs, as determined both by binding of 125I protein A and fluorescein isothiocyanate- antihuman Ig to the cells. Macrophage Fc receptors were found to be involved in the recognition of the RBCs, because phagocytosis was partially inhibited by incubating macrophages with bovine serum albumin (BSA) anti-BSA complexes, aIg (aggregated Igs), and anti-Fc receptor II monoclonal antibo * Jaffe, E.R. Chronic nonspherocytic hemolytic anemia and G6PD deficiency. Hosp.Pract.:57-70, 1991. * Lee, W.T., Flynn, T.G., Lyons, C., and Levy, H.R. Cloning of the gene and amino acid sequence for glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides. J.Biol.Chem. 266:13028-13034, 1991. Notes: Amino acid sequencing of glucose 6-phosphate dehydrogenase (Glc6PD) from Leuconostoc mesenteroides yielded sequence for over 75% of the protein. Two oligonucleotides based on the amino acid sequence were used to isolate a partial Glc6PD gene clone (pLmz-Delta-N65), from a pUC9 library, containing 85% of the coding sequence and the 3'-untranslated DNA, but lacking the 5'-noncoding DNA sequence and the portion of the gene encoding the 65 N-terminal amino acids. Attempts to obtain a full-length clone from lambda libraries were unsuccessful, possibly due to restriction of L. mesenteroides DNA by Escherichia coli host cells. The 5'-untranslated DNA was amplified by the polymerase chain reaction and partially sequenced. To obtain unmodified DNA for the gene, oligonucleotides corresponding to the 5'- and 3'-noncoding sequences were used to amplify the gene by the polymerase chain reaction, and a 1.8-kilobase pair fragment was isolated and cloned into pUC19. The recombinant plasmid, pLmz, contains the entir * MacDonald, D., Town, M., Mason, P., Vulliamy, T., Luzzatto, L., and Goff, D.K. Deficiency in red blood cells. Nature 350:115, 1991. Notes: G6PD Sunderland; Deletion of nt 102-104.

* Maeda, M. and Yoshida, A. Genetic abnormality of the CRM-negative human glucose-6-phosphate dehydrogenase variant. FASEB J. 5-ABS# 6710, 1991. * Matsuoka, N. Glucose-6-phosphate dehydrogenases of echinoderms. Comp.Biochem.Physiol. 98B:539-542, 1991. Notes: Glucose-6-phosphate dehydrogenase (G6PD) was partially purified from the brittle-star, Ophioplocus japonicus by the affinity chromatography of Blue-Sepharose CL6B. 2. The kinetic properties of some parameters were examined and compared with G6PDs from other echinoderms and various animal groups. 3. The results showed that echinoderm G6PDs varied in some kinetic parameters among groups, though they were the ordinary G6PD. * Meloni, T., Forteleoni, G., Ena, F., and Meloni, G.F. Glucose-6-phosphate dehydrogenase deficiency and bacterial infections in northern Sardinia. J.Pediatr. 118:909-911, 1991. * Meloni, T., Forteleoni, G., Noja, G., Dettori, G., Sale, M.A., and Meloni, G.F. Increased prevalence of glucose-6-phosphate dehydrogenase deficiency in patients with cholelithiasis. Acta Haematol.(Basel) 85:76-78, 1991. Notes: The glucose-6-phosphate dehydrogenase (G6PD) enzyme activity was determined in 299 Northern Sardinian patients with cholelithiasis. Sixteen (12.80%) of the 125 male patients studied were G6PD deficient; 33 (18.96%) of the 174 females were heterozygous and 1 (0.57%) homozygous. Thus, the prevalence of G6PD deficiency in male subjects with cholelithiasis is about 35% higher (p< 0.02) than that of a normal male control group (7.29%). As regards female patients, the incidence of the GdMed allele was also significantly different (p< 0.05). Thus, G6PD-deficient subjects may have a predisposition to develop gallstones, even in the absence of clinical signs of chronic hemolysis. AUTHOR. * Meloni, T., Forteleoni, G., and Porcu, A. Acute hemolytic anemia in two G6PD-deficiency children with viral hepatitis. Haematologica (Pavia) 73:397-399, 1991. * Missiou-Tsagaraki, S. Screening for glucose-6-phosphate dehydrogenase deficiency as a preventive measure: Prevalence among 1,286,000 Greek newborn infants. J.Pediatr. 119:293-299, 1991. Notes: We evaluated the Greek screening program for glucose-6-phosphate dehydrogenase (G6PD) deficiency, which was incorporated into the existing national phenyketonuria (PKU) screening program to identify infants with G6PD deficiency and eliminate the induction of acute hemolytic crisis by informing the families about the extrinsic factors that G6PD-deficient patients should avoid. Between 1977 and 1989, 1,286,000 infants were screened. The fluorescent spot test was used on samples extracted from dried blood spots. Abnormal fluorescence due to G6PD deficiency (severe or partial) was found in 3.14% of the samples (1 in 22 males and 1 in 54 females). The sensitivity of the test for homozygosity and hemizygosity was 100%. In heterozygosity the test identifies only subjects who have considerably diminished enzyme activity. The test is inexpensive when added to the PKU screening program ($0.90 US per test). We believe that screening a population tar G6PD deficiency is justified if the incidence of the deficien * Modiano, G., Ciminelli, B.M., Malaspina, P., Santolamazza, P., Sedran, L., Meloni, T., Forteleoni, G., and Mela, G. A further polymorphism of the Gd locus for glucose-6-phosphate dehydrogenase present among blacks (Nigerians) and apparently absent among Caucasoids: The quantitative isoelectrophoretic

variation of the Gd+ allele. Hum.Hered. 41:353-363, 1991. Notes: A structural but isoelectrophoretic moderate variation of glucose-6-phosphate dehydrogenase (G6PD) activity is common among Nigerians (a black population exposed to a long-lasting intense Plasmodium falciparum malarial endemia). It had never even been searched for among Caucasoids and Mongoloids. In the present work, we attempted to ascertain whether this polymorphism exists among Caucasoids. With this purpose, two Caucasoid male populations were studied: Sardinians and Romans, who respectively did and did not experience an evolutionarily effective exposure to P. falciparum. The approach adopted here consisted in comparing the variations of G6PD activity observed between brothers who certainly received their Gd gene from the same grandparent (hence Gd genes identical by descent) with those between brothers who received it (in the Roman series) or may have received it (in the Sardinian series) from different grandparents. No evidence for common moderate G6PD activity variations segregating with the G * Monte Alegre, S., Saad, S.T.O., Delatre, E., and Saad, M.J.A. Insulin secretion in patients deficient in glucose-6-phosphate dehydrogenase. Horm.Metab.Res. 23:171-173, 1991. Notes: Intravenous (IVGTT) and oral glucose tolerance tests (OGTT) were carried out in 12 men with glucose-6-phosphate dehydrogenase (G-6-PD) deficiency and in 11 normal men. The race, the mean age and body mass index were similar in the G-6-PD deficient and in the normal men. No significant differences were demonstrated between mean plasma glucose levels in the C-6-PD deficient subjects and those in the normal men during IVGTT and OGTT. In contrast the insulin levels were significantly lower for the G-6-PD deficient subjects as compared to the controls at 30 minutes (P< 0.04) in the OGTT and at 1 min (P< 0.001), 3 min (P< 0.001), 5 min (P< 0.001) and 10 minutes (P< 0.002) in the IVGTT. All indexes of first phase insulin release were also significantly (P< 0.001) lower in G-6-PD deficient men. These results emphasize the metabolic importance of G-6-PD in the process of glucose induced insulin release. AUTHOR. * Niazi, G.A. Glucose-6-phosphate dehydrogenase deficiency and diabetes mellitus. Int.J.Hematol. 54:295-298, 1991. Notes: This hospital-based study demonstrates a statistically significant higher prevalence of glucose-6-phosphate dehydrogenase (G6PD) deficiency among the Saudi patients with diabetes mellitus (12.4%) as compared to healthy population controls (2.0%) (p less than 0.008). The nature of this association is difficult to explain. In view of a higher frequency of G6PD deficiency among diabetics, it is suggested that all patients with diabetes be screened for this enzymopathy in order to avoid the use of certain drugs or toxic agents that can produce hemolysis. * Ninfali, P., Bresolin, N., Baronciani, L., Fortunato, F., Comi, G., Magnani, M., and Scarlato, G. Glucose-6-phosphate dehydrogenase Lodi844C: A study on its expression in blood cells and muscle. Enzyme 45:180-187, 1991. Notes: Glucose-6-phosphate dehydrogenase (G6PD) deficiency was found in erythrocytes, lymphocytes and muscle of an Italian male. whose family has lived for at least three generations in Lodi (Lombardy, northern Italy). The subject was hospitalized for myalgia and dark urine after intense physical exercise, but no sign of anemia and chronic hemolysis were present at rest. Family studies revealed that the mother and the maternal aunt had the

same enzymopathy. The enzyme-specific activity in red blood cells was 15% of control and the kinetic properties were the following: slower electrophoretic mobility; biphasic pH activity curve; slightly reduced thermal stability, and increased utilization of the substrate analogs. The analysis of our patient's DNA showed a G ==> C mutation at nucleotide 844 which causes an Asp ==> His amino acid change in position 282. This is the same mutation found by De Vita et al. in the G6PD Seattle-like variant. However, by following a new convention, we labelled our variant as G6PD * zsoylu, S. Glucose-6-phosphate dehydrogenase deficiency. N.Engl.J.Med. 324:1743, 1991. * Persson, B., Jrnvall, H., Wood, I., and Jeffery, J. Functionally important regions of glucose-6-phosphate dehydrogenase defined by the Saccharomyces cerevisiae enzyme and its differences from the mammalian and insect forms. Eur.J.Biochem. 198:485-491, 1991. Notes: The primary structure of Saccharomyces cerevisiae glucose6-phosphate dehydrogenase has been determined. It consists of 503 amino acid residues, with an acetyl-blocked N-terminus. The structure shows equally extensive differences from the corresponding mammalian and fruit fly enzymes (52% residues non-identical). Residues conserved in all the forms constitute about 40% of the structures and include two histidines. One of these (His200 in the numbering of the rat enzyme) occurs in a 10-residue conserved segment, including the reactive Lys204, probably related to substrate binding. Two segments with conserved Gly-Xaa-Xaa-Gly- Xaa-Xaa-Gly/Ala pattern constitute possibilities for the coenzyme- binding site. One is N-terminally located (positions 37-43) with two conserved arginine residues nearby (positions 56 and 71). of interest for phosphate binding. The other (positions 241-247) is in a middle region. with many residue identities, containing the conserved residues Arg256 and His264. AUTHOR. * Poon, M.-C., Prchal, J., and Beutler, E. Unpublished , 1991. Notes: G6PD Calgary. 1178A. Physician=Poon/Prchal. Patient=Michael Dole. * Reid, H.L., Bharaj, B.S., Asemota, H.N., and St.Morrison, E.Y. Increased erythrocyte glucose-6-phosphate dehydrogenase, 2,3-bisphosphoglycerate and whole blood reduced glutathione levels in black diabetics. Med.Sci.Res. 19:419-420, 1991. * Rowley, D.L. and Wolf, R.E.,Jr. Molecular characterization of the Escherichia coli K-12 zwf gene encoding glucose 6-phosphate dehydrogenase. J.Bacteriol. 173:968-977, 1991. Notes: In Escherichia coli K-12, expression of zwf, the gene for glucose 6- phosphate dehydrogenase, is coordinated with the cellular growth rate and induced by superoxide-generating agents. To initiate the study of the molecular mechanisms regulating its expression, the gene was cloned and its DNA sequence was determined. The 5' ends of zwf mRNA isolated from cells growing in glucose and acetate minimal media were mapped. The map was complex in that transcripts mapped to -45, -52, and -62, with respect to the beginning of the coding sequence. Three analytical methods were used to search the DNA sequence for putative promoters. Only one sequence for a promoter recognized by the sigma-70 form of RNA polymerase was found by all three search routines that could be aligned with a mapped transcript, indicating that the other transcripts arise by processing of the mRNA. A computer-assisted search did not reveal a

thermodynamically stable long- range mRNA secondary structure that is capable of sequestering the tr * Saad, M.J.A., Monte-Alegre, S., and Saad, S.T.O. Cortisol levels in glucose-6-phosphate dehydrogenase deficiency. Horm.Res. 35:1-3, 1991. Notes: The aim of the present study was to investigate cortisol levels under basal conditions and in response to ACTH stimulation in male patients with glucose-6-phosphate dehydrogenase (G-6-PD) deficiency. The study included 14 male controls and 12 patients with G-6-PD deficiency matched for age and race. Fasting blood samples were taken from all the subjects at rest, and 30, 60 and 120 min after the infusion of 0.25 mg of corticotropin for cortisol determination. The mean cortisol levels observed in the first hour after ACTH stimulation in the G-6- PD-deficient patients were significantly (p = 0.03) lower than in the control group. No significant differences were observed between patients and controls at rest, and in the second hour after stimulation. These data suggest that, in the adrenals, G-6-PD plays a role in the initial phase of cortisol production. However, 1 h after ACTH stimulation, G-6-PD probably is no longer rate limiting in the production of cortisol. AUTHOR. * Saha, N. and Samuel, A.P.W. Characterization of glucose-6-phosphate dehydrogenase variants in the Sudan--including GdKhartoum, a hyperactive slow variant. Hum.Hered. 41:17-21, 1991. * Saleem, T.H., Mendis, B.S., and Osanyintuyi, S.O. Glucose-6-phosphate dehydrogenase deficiency in a rural Saudi population. J.Trop.Med.Hyg. 94:327-328, 1991. * Scott, M.D., Zuo, L., Lubin, B.H., and Chiu, D.T.-Y. NADPH, not glutathione, status modulates oxidant sensitivity in normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes. Blood 77:2059-2064, 1991. Notes: Glucose-6-phosphate dehydrogenase (G6PD) deficiency is characterized by the loss of NADPH and enhanced erythrocyte oxidant sensitivity. Historically, it has been theorized that the elevated oxidant sensitivity of G6PD-deficient erythrocytes arises as the direct consequence of decreased intracellular glutathione (GSH) concentrations. To directly investigate the basis of G6PD deficiency oxidant sensitivity, the effects of altered GSH and NADPH concentrations were examined in normal and G6PD-deficient erythrocytes. The results of this study demonstrated that GSH depletion, by 1-chloro-2,4-dinitrobenzene (CDNB), had no effect on hemoglobin oxidation in response to hydrogen peroxide (H2O2) generating systems )phenazine methosulfate and menadione bisulfite) in either normal or G6PD-deficient cells. Furthermore, a fourfold to sixfold increase in intracellular GSH concentration also did not protect against H2O2-generating systems in the normal or G6PD-deficient erythrocytes. Conversely, introduction of an N * Shimizu, Y., Kawarada, S.-Y., Suzuki, M., and Tanaka, T. Interstrain differences in red cell enzyme activities in mice and rats. Comp.Biochem.Physiol.[B] 100B:687-690, 1991. Notes: Interstrain differences in red blood cell enzyme activities were studied in mice (BALB/c, C57BL/6, C3H/He, DBA/2 and ddY) and rats (Donryu, F344/N, SD, Wistar and Wistar/ST), and were also compared with hamster, guinea- pig and rabbit. The enzyme activities measured were: glutathione S-transferase (GST), gIucose-6-phosphate dehydrogenase (G-6-PD), 6-phosphogluconate dehydrogenase (6-PGD), NADPH-diaphorase (ND), hexokinase (Hx), glutamate oxaloacetate transaminase (GOT), lactate dehydrogenase

(LDH) and acetylcholinesterase (AChE). There were marked variations in the activities of some red cell enzymes (e.g. GST, Hx, ND), while others (e.g. G-6-PD, 6- PGD) were much less variable both within different strains and species. AUTHOR. * Shimizu, Y. and Suzuki, M. The relationship between red cell aging and enzyme activities in experimental animals. Comp.Biochem.Physiol. 99B:313-316, 1991. Notes: 1. The relationship between red cell aging and enzyme activities was studied in rabbit, guinea-pig, hamster, rats (F344/N and SD), and mice (BALB/c and DBA/2). 2. The activities of six enzymes: glucose-6-phosphate dehydrogenase (G-6- PD), 6-phosphogluconate dehydrogenase (6-PGD), hexokinase (Hx), glutamate oxaloacetate transminase (GOT), lactate dehydrogenase (LDH) and acetylcholinesterase (AChE), were measured in the red cells of different ages which were obtained either by centrifugation or experimental anaemia. 3. Hx, AChE and GOT activities were much higher in younger red cells than in older cells, hence the activities of these enzymes may be used as an indicator of age of the cells. AUTHOR. * Simofuruya, H. and Suzuki, J. Determination of nucleoside triphosphates by use of combined reactions of hexokinase and glucose-6-phosphate dehydrogenase. Biochem.Int. 25:1071-1076, 1991. Notes: ATP is known to be easily determined fluorometrically after it is utilized to produce the corresponding amount of NADPH by combined reactions of hexokinase and glucose6-phosphate dehydrogenase. We studied further whether nucleoside triphosphates other than ATP can be also determined in a similar manner if they were incubated for a longer period with an increased amount of hexokinase. It was shown that CTP, GTP, ITP, and UTP can be utilized to produce the corresponding amount of NADPH after an incubation of at least 60 min and that 0 to 50 nmols of these nucleotides were able to be determined fluorometrically. Copyright 1992 Academic Press, Inc. * Stanton, R.C., Seifter, J.L., Boxer, D.C., Zimmerman, E., and Cantley, L.C. Rapid release of bound glucose-6-phosphate dehydrogenase by growth factors. Correlation with increased enzymatic activity. J.Biol.Chem. 266:12442-12448, 1991. Notes: Epidermal growth factor (EGF), a mitogen for renal proximal tubule cells, activated the hexose monophosphate (HMP) shunt in renal proximal tubule cells (Stanton, R. C., and Seifter, J. L. (1988) Am. J. Physiol. 254, C267-C271). We therefore evaluated the effect of EGF on the HMP shunt enzymes glucose 6-phosphate dehydrogenase (G6PD, the rate-limiting enzyme) and 6-phosphogluconate dehydrogenase. Rat renal cortical cells (RCC) were incubated with either EGF or platelet-derived growth factor (PDGF) and then assayed for G6PD and 6-phosphogluconate dehydrogenase activities. EGF and PDGF increased G6PD activity by 25 and 27% respectively. Although phorbol myristate acetate (PMA), ionomycin, PMA+ ionomycin, and 8-bromo-cyclic AMP had no significant effect on the activity, a 5-min preincubation with PMA potentiated the activation of G6PD by PDGF. Growth factor activation of G6PD was also seen in a fibroblast and epithelial cell line. None of the agents affected 6- phosphogluconate dehydrogenase activity in * Stocco dos Santos, R.C., Barretto, O.C.O., Nonoyama, K., Castro, N.H.C., Ferraz, O.P., Walter-Moura, J., Vescio, C.C.S., and Be ak, W. X-linked syndrome: Mental retardation, hip luxation, and G6PD variant [Gd(+) Butantan]. Am.J.Med.Genet. 39:133-136, 1991.

Notes: An apparently new X-linked syndrome is presented. It occurred in four male first cousins. The main manifestations of this syndrome are severe mental retardation, bilateral congenital hip luxation, and short stature. Three of the affected males showed a new glucose-6-phosphate dehydrogenase variant. AUTHOR. * Storey, K.B., Keefe, D., Kourtz, L., and Storey, J.M. Glucose-6-phosphate dehydrogenase in cold hardy insects: Kinetic properties, freezing stabilization, and control of hexose monophosphate shunt activity. Insect Biochem. 21:157-164, 1991. * Tagarelli, A., Bastone, L., Cittadella, R., Calabro, V., Bria, M., and Brancati, C. Glucose-6-phosphate dehydrogenase (G6PD) deficiency in Southern Italy: A study on the population of the Cosenza province. Gene Geography 5:141-150, 1991. * Tang, T.K., Huang, C.-S., Huang, M.-J., Tam, K.-B., and Tang, C.-J.C. Identification and diagnosis of glucose-6-phosphate dehydrogenase (G6PD) mutations in Chinese. Blood 78:86a, 1991. * Teel, J.F., Kletzien, R.F., Ginsberg, L.C., Stevens, G.J., and Stapleton, S.R. Acetaldehyde increases mRNA levels of glucose-6-phosphate dehydrogenase in rat hepatocytes in culture. FASEB J. 5:A424-ABS# 310, 1991. * Todisco, V., Lamour, J., and Finberg, L. Hemolysis from exposure to naphthalene mothballs. N.Engl.J.Med. 325:1660, 1991. * Toniolo, D., Filippi, M., Dono, R., Lettieri, T., and Martini, G. The CpG island in the 5' region of the G6PD gene of man and mouse. Gene 102:197-203, 1991. Notes: The nucleotide (nt) sequence of the entire CpG island in the 5' region of the human glucose-6-phosphate dehydrogenaseencoding gene (G6PD) and of the corresponding region in mouse was determined. In comparison to the human gene, the 5' region of the mouse G6PD gene has highly reduced G + C and CpG dinucleotide content, but maintains the functional features of a CpG island, as it is differentially methylated on the active vs. the inactive X chromosome. In addition to the expected conservation of exons, nt sequence comparison showed that several boxes are highly conserved between the two species in the 5' flanking DNA and in the first intron. Moreover, the conservation of the position of most CpG dinucleotides in the promoter region and in one of the upstream boxes, at about -900, gives support to the hypothesis that, in each island, specific CpGs play a major role in the regulation of gene expression. AUTHOR. * Tranulis, M.A., Christophersen, B., Blom, A.K., and Borrebaek, B. Glucose dehydrogenase, glucose-6-phosphate dehydrogenase and hexokinase in liver of rainbow trout (Salmo gairdneri). Effects of starvation and temperature variations. Comp.Biochem.Physiol. 99B:687-691, 1991. Notes: Activities of trout liver glucose dehydrogenase (GDH, EC 1.1.1.47) and glucose-6-phosphate dehydrogenase (G6PD. EC 1.1.1.49) were increased after a sudden drop in water temperature, but not in long-time cold acclimated as compared with warm acclimated trout. Possibly, the activities of GDH and G6PD were temporarily increased in connection with metabolic adaptation to the lower temperature. The activities of GDH and G6PD were not changed by the stress of handling. Partially purified trout liver GDH has a lower activation energy with glucose than with glucose-6-phosphate as substrate, and the K (glucose) decreases with decreasing assay temperature. At low temperatures, the activity of trout liver GDH with glucose as substrate may be comparable to that of glucose- 6-phosphate. Partially purified beef liver GDH has a high activation energy with glucose as substrate, and the Km (glucose) does not change

with the assay temperature. Hexokinase (HK, EC 2.7.1.1) and GDH activities were unchanged when trout w * Vives Corrons, J.-L., Garcia, A.M., Sosa, A.M., Pujades, A., Colomer, D., and Linares, M. Heterozygous pyruvate kinase deficiency and severe hemolytic anemia in a pregnant woman with concomitant, glucose-6-phosphate dehydrogenase deficiency. Blut 62:190-193, 1991. Notes: The aim of this paper is to describe the clinical and hematological characteristics of a 32-year-old woman with concomitant heterozygous pyruvate kinase (PK) and glucose-6-phosphate dehydrogenase (G6PP) deficiencies and severe hemolytic anemia during pregnancy. In 1964, Oski et al. [16] described a family in which a clinically healthy woman was heterozygous for both PK and G6PD deficiencies. To our knowledge, the present case is the first described in which the same condition is associated with hemolysis. A heterozygous condition for both enzymopathies was clearly demonstrated by family study criteria, and all other causes of hemolytic anemia were eliminated. No evidence of genetic relationship between the two disorders was demonstrated. Since late onset of hemolysis in heterozygous PK-deficient women has been observed in association with pregnancy and the molecular characteristics of the concomitant deficient G6PD enzyme were kinetically favorable, partial PK deficiency is suggested as the major ca * Vulliamy, T.J., Othman, A., Town, M., Nathwani, A., Falusi, A.G., Mason, P.J., and Luzzatto, L. Polymorphic sites in the African population detected by sequence analysis of the glucose-6-phosphate dehydrogenase gene outline the evolution of the variants A and A-. Proc.Natl.Acad.Sci.USA 88:8568-8571, 1991. Notes: The human X chromosome-linked gene encoding glucose-6-phosphate dehydrogenase (C6PP; EC 1.1.1.49) is known to be highly polymorphic from the biochemical characterization of enzyme variants. The variant A (with enzyme activity in the normal range) and the variant A- (associated with enzyme deficiency) each have a frequency of about 0.2 in several African populations. Two restriction fragment length polymorphisms have also been found in people of African descent, but not in other populations, whereas a silent mutation has been shown to be polymorphic in Mediterranean, Middle Eastern, African, and Indian populations. We report now on two additional polymorphisms that we have detected by sequence analysis, one in intron 7 and one in intron 8. The analysis of 54 African male subjects for the seven polymorphic sites, clustered within 3 kilobases of the G6PD gene, has revealed only 7 of the 128 possible haplotypes, indicating marked linkage disequilibrium. These data have enabled us to suggest an evolution * Yaish, H.M., Niazi, G.A., Al Shaalan, M., Khan, S., and Ahmad, S. Increased incidence of hyperbilirubinemia in "unchallenged" glucose-6-phosphate dehydrogenase deficiency in term newborns. Ann.Trop.Pediatr. 11:259-266, 1991. * Anonymous Pyruvate kinase deficiency. Association with G6PD deficiency . BMJ 305:760-762, 1992. * Ahluwalia, A., Corcoran, C.M., Vulliamy, T.J., Ishwad, C.S., Naidu, J.M., Argusti, A., Stevens, D.J., Mason, P.J., and Luzzatto, L. G6PD Kalyan and G6PD Kerala; two deficient variants in India caused by the same 317 Glu-->Lys mutation. Hum.Mol.Genet.. 1:209-210, 1992. * Bautista, J.M., Mason, P.J., and Luzzatto, L. Purification and properties of human glucose-6-phosphate dehydrogenase made

in E. coli. Biochim.Biophys.Acta 1119:74-80, 1992. Notes: The cDNA for the X-chromosome encoded human glucose-6phosphate dehydrogenase (G6PD) has been expressed in E. coli and the enzyme purified to homogeneity, using a simple one-step fractionation on 2'5'-ADP-Sepharose. By selecting one of several different expression vectors and by optimizing culture conditions a yield of more than 10 mg of pure enzyme per liter of culture is obtained reproducibly. When the recombinant enzyme and authentic G6PD purified from normal human red cells were compared, they proved to be indistinguishable by the following criteria: electrophoretic mobility in both native and denaturing conditions, the Km values for glucose 6-phosphate and NADP and the Ki value for NADPH. The recombinant enzyme, unlike the red cell enzyme, retained 100% activity when stored at 4 C for over 1 year. AUTHOR. * Beutler, E., Westwood, B., Kuhl, W., and Hsia, Y.E. Glucose-6-phosphate dehydrogenase variants in Hawaii. Hum.Hered. 42:327-329, 1992. Notes: (MS330) (B940) Sequence analysis has been performed on the DNA of 13 glucose- 6-phosphate dehydrogenase (G6PD) deficient males from Hawaii, 6 of Filipino, 6 of Laotian, and 1 of Chinese extraction. Four different mutations were found: A --> T at cDNA nt 835, G --> A at nt 871, C --> T at nt 1360, and G -- > A at nt 1388. The mutations at nt 835 and nt 1360 have not been described previously, and the latter, in particular, appears to be relatively common. The nt 1360 mutation changes the same codon as is altered in a previously described mutation, G6PD Andalus. AUTHOR. * Beutler, E. and Westwood, B. Unpublished , 1992. * Beutler, E. Molecular biology of G6PD variants and other red cell enzyme defects. Ann.Rev.Med. 43:47-59, 1992. Notes: (MS292) (B917). * Beutler, E. Glucose-6-phosphate dehydrogenase deficiency: 1953-1992. Sangre (Barc.) 37:15-20, 1992. Notes: (MS320) (B936). * Beutler, E. and Kuhl, W. Variability and population genetics of G6PD. In: Genetic Diversity Among Jews: Diseases and Markers at the DNA Level, edited by Bonne-Tamir, B. and Adam, A.New York:Oxford University Press, 1992,p. 60-69. Notes: (MS283) (B923). * Beutler, E., Kuhl, W., Fox, M., Tabsh, K., and Crandall, B.F. Prenatal diagnosis of glucose-6-P dehydrogenase (G6PD) deficiency. Acta Haematol.(Basel) 87:103-104, 1992. Notes: (MS301) (B921). * Beutler, E., Westwood, B., and Sipe, B. A new polymorphic site in the G6PD gene. Hum.Genet. 89:485-486, 1992. Notes: (MS328) (B932) A polymorphic restriction site has been found in intron 11 of the gene for glucose-6-phosphate dehydrogenase (G6PD). This site is produced by a T-C substitution 13 bp upstream of exon 12, producing an NlaIII restriction site. In various populations there was a strong association between a T at nt 1311 of the G6PD cDNA and the presence of the NlaIII restriction site. Among African Americans, however the presence of a C at nt 1311 was sometimes associated with the presence of a polymorphic NlaIII site. AUTHOR. * Beutler, E., Westwood, B., Prchal, J., Vaca, G., Bartsocas, C.S., and Baronciani, L. New glucose-6-phosphate dehydrogenase mutations from various ethnic groups. Blood 80:255-256, 1992. Notes: MS335 (B930). * Brown, A.K. Hyperbilirubinemia in black infants: Role of

glucose-6-phosphate dehydrogenase deficiency. Clin.Pediatr. 31:712-715, 1992. * Chang, J.-G., Chiou, S.-S., Perng, L.-I., Chen, T.-C., Liu, T.-C., Lee, L.-S., Chen, P.-H., and Tang, T.K. Molecular characterization of glucose-6-phosphate dehydrogenase (G6PD) deficiency by natural and amplification created restriction sites: Five mutations account for most G6PD deficiency cases in Taiwan. Blood 80:1079-1082, 1992. Notes: We have developed a rapid and simple method to diagnose the molecular defects of glucose-6-phosphate dehydrogenase (G6PD) deficiency in Chinese in Taiwan. This method involves the selective amplification of a DNA fragment from human G6PD gene with specific oligonucleotide primers followed by digestion with restriction enzymes that recognize artificially created or naturally occurring restriction sites. Ninety- four Chinese males with G6PD deficiency were studied. The results show that 50% (47 of 94) were G to T mutation at nucleotide (nt) 1376,21.3% (20 of 94) were G to A mutation at nt 1388,7.4% (7 of 94) were A to G mutation at nt 493, 7.4% (7 of 94) were A to G mutation at nt 95.4.2% (4 of 94) were C to T mutation at nt 1024, 1.1% (1 of 94) was G to T mutation at nt 392, and 1.1% (1 of 94) was G to A mutation at nt 487. These results show that the former five mutations account for more than 90% of G6PD deficiency cases in Taiwan. Aside from showing that G to T change at nt 1376 is the most common * Chongxing, N., Shuangxing, Z., and Yiqin, L. Microdetermination of G6PD isoenzyme activity in human erythrocytes by thin-layer PAG-IEF. J.Biochem.Biophys.Methods 25:245-251, 1992. Notes: An improved method of mierodetermination of G6PD isoenzyme activity in human erythrocvtes was developed by modification of previously reported procedures. The volume of blood samples was reduced from 2 ml to 20 H1 After hemolysis in 2% Triton X-100 and 0.1% beta-mereaptoethanol, the samples were subjected to centrifugation and thin-layer isoelectric focusing in polyacrylamide gel (PAG-IEF). By comparison with the original method, excellent resolution was obtained by this more rapid and simple procedure. AUTHOR. * Choudhry, V.P., Bagga, A., and Desai, N. Increased morbidity following acute viral hepatitis in children with glucose-6-phosphate dehydrogenase deficiency. J.Trop.Pediatr. 38:139-140, 1992. * Coetzee, M.J., Bartleet, S.C., Ramsay, M., and Jenkins, T. Glucose-6-phosphate dehydrogenase (G6PD) electrophoretic variants and the PvuII polymorphism in Southern African populations. Hum.Genet. 89:111-113, 1992. Notes: Southern African Bantu-speaking negroid and San populations were examined with regard to the glucose-6-phosphate dehydrogenase (G6PD) PvuII restriction fragment length polymorphism (RFLP) showing alleles of 4 kb and 1.6 kb, called Type 1 and Type 2, respectively. The standardized disequilibrium coefficient for the electrophoretic G6PD types and PvuII alleles in the Southern African population was 0.28. The molecular lesion causing the Gd(A) mutation is the same in the San and Southern African negroid populations. Gd(A) chromosomes are found in association with both the Type 1 and Type 2 alleles, whereas none of the 62 Gd(B) chromosomes from the Southern African populations had the Type 2 allele. Five of the 44 Gd(B) chromosomes studied in the American Black population had the Type 2 allele, indicating that the Gd(B) allele in the two populations may have

different origins. The presence of all 3 A- deficiency mutations in the G6PD A gene, in a region where the ancestral population was thought to have * Corcoran, C.M., Calabro, V., Tamagnini, G., Town, M., Haidar, B., Vulliamy, T.J., Mason, P.J., and Luzzatto, L. Molecular heterogeneity underlying the G6PD Mediterranean phenotype. Hum.Genet. 88:688-690, 1992. Notes: As part of a study aiming to define the molecular basis of glucose-6-phosphate dehydrogenase (G6PD) deficiency, we analysed a sample from a Portugese boy with a family history of favism. Although the biochemical properties of red-cell G6PD from this subject were similar to those of the common variant G6PD Mediterranean, the corresponding mutation (563 C-->T) was not present. Instead, polymerase chain reaction (PCR) amplification and sequencing of the entire gene detected a C-->T transition at nucleotide 592 in exon VI, changing an arginine residue to a cysteine residue only 10 amino acids downstream from the Mediterranean mutation. Single-strand conformation polymorphism analysis of a PCR- amplified DNA fragment spanning exons VI and VII of the G6PD gene has detected the same mutation, confirmed by sequencing, in a G6PD-deficient patient from Southern Italy. We name this new variant G6PD Coimbra. AUTHOR. * Curnutte, J.T., Hopkins, P.J., Kuhl, W., and Beutler, E. Studying X-inactivation. Lancet 339:749, 1992. Notes: (MS345) (B915). * De Wardener, H.E. From a third factor to a glucose-6-phosphate dehydrogenase stimulator. Contrib.Nephrol. 100:172-187, 1992. * Du, C.S., Chao, L.T., Louie, E., Liu, T.Z., and Chiu, D.T.Y. Molecular characterization of G6PD deficiency in patients of Chinese descent and identification of a new base substitution in the human G6PD gene. Blood 80 (Suppl 1):284a, 1992. * Ferretti, A., Bozzi, A., Di Vito, M., Podo, F., and Strom, R. 13C and 31P NMR studies of glucose and 2-deoxyglucose metabolism in normal and enzyme-deficient human erythrocytes. Clin.Chim.Acta 208:39-61, 1992. Notes: The flux of 13C-labeled glucose through the Embden-Meyerhof and pentose phosphate pathways was studied by 13C NMR in intact erythrocytes isolated from normal subjects or from patients suffering of glucose-6-phosphate dehydrogenase (G6PD, EC 1.1.1.49) deficiency. Similar rates of glucose catabolism and similar fluxes of the 13C-label into 2,3- bisphosphoglycerate and lactate were found, under basal conditions, in normal and in G6PD-deficient erythrocytes incubated in the presence of either [1 -13C]- or D-[6- 13C]glucose. Exposure to oxidative stress by preincubation with tert-butylhydroperoxide induced in normal, but not in G6PD- deficient erythrocytes, a significant enhancement of glucose consumption, as well as a substantial reduction in 13C-label transfer from C1-glucose into lactate. It was also possible, by 31P NMR, to evaluate the conversion of 2-deoxyglucose to its phosphate-containing metabolites. The oxidation and subsequent decarboxylation of 2-deoxyglucose6-phosphate was assessed in reco * Filosa, S., Calabro, V., Vallone, D., Poggi, V., Mason, P., Pagnini, D., Alfinito, F., Rotoli, B., Martini, G., Luzzatto, L., and Battistuzzi, G. Molecular basis of chronic non-spherocytic haemolytic anaemia: A new G6PD variant (393 Arg-->His) with abnormal KmGPD and marked instability. Br.J.Haematol. 80:111-116, 1992. Notes: More than 80 genetic variants of glucose-6-phosphate

dehydrogenase (G6PD) are associated with chronic non- spherocytic haemolytic anaemia (CNSHA). In order to help clarify the molecular basis of this association, we have carried out a detailed biochemical and genetic characterization of two G6PD deficient brothers affected by CNSHA. The G6PD from the two patients has altered electrophoretic mobility, abnormally elevated Michaelis constant (Km) for G6P, and extreme instability in vivo and in vitro. By comparison with published information we found that this is a new G6PD variant which we have designated G6PD Portici. The entire coding region of the gene has been sequenced, and a single point mutation, a G-->A transition, was found at position 1178 in exon X, causing a substitution of histidine for arginine at residue 393 in the polypeptide chain. By polymerase chain reaction (PCR) amplification followed by diagnostic restriction enzyme analysis and allele- specific oligonucleotide hybridization we ha * Hirono, A., Fujii, H., Hirono, K., Kanno, H., and Miwa, S. Molecular abnormality of a Japanese glucose-6-phosphate dehydrogenase variant (G6PD Tokyo) associated with hereditary non-spherocytic hemolytic anemia. Hum.Genet. 88:347-348, 1992. Notes: The entire coding sequence of a Japanese class 1 variant (G6PD Tokyo) was amplified by the polymerase chain reaction from genomic DNA. Nucleotide analysis by a direct sequencing technique revealed a unique nucleotide substitution (1246 G to A) in exon 10, which predicts a Glu to Lys substitution at the 416th amino acid. This is another member of a conspicuous mutation cluster surrounding the putative NADP-binding domain. AUTHOR. * Hirono, A., Fujii, H., and Miwa, S. Molecular abnormality of G6PD Konan and G6PD Ube. Hum. Genet. 1992.(In Press) * Hsia, Y.E., Miyakawa, F., Baltazar, J., Ching, N.S.P., and Beutler, E. Frequency of G6PD mutations in Chinese, Filipinos and Laotians. Am.J.Hum.Genet. 51:151a, 1992. Notes: (B948). * Huang, C.-S., Tang, C.-J.C., Huang, M.-J., and Tang, T.K. Diagnosis of glucose-6-phosphate dehydrogenase (G6PD) mutations by DNA amplification and allele-specific oligonucleotide probes. Acta Haematol.(Basel) 88:92-95, 1992. Notes: We have recently identified that at least four types of mutation are responsible for the glucose-6-phosphate dehydrogenase (G6PD) polymorphism in the Chinese of Taiwan. Two mutations (487 G-->A and 493 A-->G) occurring at nucleotide position 487 and 493, respectively, create AIu I and Ava II recognition sites which enabled us to directly examine these two mutations by PCR/restriction enzyme (RE) digestion. However, the other two mutations (1376 G-->T and 1388 G-->A), which do not generate any recognizable restriction sites, were detected by DNA sequencing method which is not suitable for rapid diagnosis. Using the PCR technique, we have successfully developed a simple and rapid method for the detection of 1376 and 1388 mutations. This method involves the selective amplification of a DNA fragment from human G6PD gene with specific oligonucleotide primers, followed by hybridization with allele-specific oligonucleotide (ASO) probes. Using the PCR/ASO and PCR/RE methods, we have successfully examined tw * Hussein, L., Yamamah, G., and Saleh, A. Glucose-6-phosphate dehydrogenase deficiency and sulfadimidin acetylation phenotypes in Egyptian oases. Biochem.Genet. 30:113-121, 1992. Notes: Screening of 1315 males from two Egyptian oases for glucose- 6-phosphate dehydrogenase deficiency (G-6PD) found an incidence of 5.9%. The rate of acetylation of sulfadimidin was

also studied, and a bimodal distribution was found with 73% rapid acetylators. There is a correlation between high frequency of G-6PD deficiency and high frequency of slow acetylation rate. AUTHOR. * Kaplan, M., Abramov, A., and Hammerman, C. Screening for glucose-6-phosphate dehydrogenase deficiency. J.Pediatr. 121:165-166, 1992. * Kaplan, M. and Abramov, A. Neonatal hyperbilirubinemia associated with glucose-6-phosphate dehydrogenase deficiency in Sephardic-Jewish neonates: Incidence, severity, and the effect of phototherapy. Pediatrics 90:401-405, 1992. Notes: Glucose-6-phosphate dehydrogenase (G-6-PD) deficiency is frequently associated with neonatal hyperbilirubinemia, and sometimes kernicterus, often in the absence of any identifiable trigger or hematological evidence of hemolysis. The aim of this study was to compare the incidence and severity of, and the effect of phototherapy on, jaundice in G-6-PD- deficient vs G-6-PD-normal neonates in the Sephardic-Jewish community. Healthy term newborns, born to mothers of families stemming from geographic areas known to be "at risk" for G-6-PD deficiency, were screened for the condition and surveyed for hyperbilirubinemia. Seventy-five G-6-PD-deficient neonates formed the study group, while 266 neonates with normal levels of the enzyme formed the control group. Neonates with any other identifiable cause for jaundice were excluded. Phototherapy was commenced when the serum bilirubin levels reached 16 mg/dL (274 umol/L) or more, and it was discontinued at 12 mg/dL (205 pmol/L) or less. Hyperbilirubinemia develope * Kar, S., Seth, S., and Seth, P.K. Prevalence of malaria in Ao Nagas and its association with G6PD and HbE. Hum.Biol. 64:187-197, 1992. Notes: * The data suggest that malaria is an important ecologic factor in maintaining the high frequency of G6PD deficiency and HbE among the Ao Nagas. Although migrations from adjoining populations that have a high frequency of both these traits could have contributed to the presence of these genes in the Ao Nagas, malaria also could be an essential determinant in maintaining the current high frequency in present-day Ao Nagas. * Kay, A.C., Kuhl, W., Prchal, J.T., and Beutler, E. The origin of G6PD polymorphisms in Afro-Americans. Am.J.Hum.Genet. 50:394-398, 1992. Notes: (MS318)(B909). * Kuliszkiewicz-Janus, M., Tyran, W., and Szajerka, G. Haemolytic crises caused by Hoya carnosa in a patient with G6PD deficiency. Acta Haematol.Pol. 23:63-67, 1992. Notes: Haemolytic crises caused by contact with Hoya carnosa were observed in a 45-years old woman. The investigation of erythrocyte enzymes displayed both G6PD deficiency and its diminished affinity to G-6-P. Some properties of dehydrogenases isolated from erythrocytes of the patient's brother and son were also changed although clinical signs of haemolysis were absent. * Maeda, M., Constantoulakis, P., Chen, C.-S., Stamatoyannopoulos, G., and Yoshida, A. Molecular abnormalities of a human glucose-6-phosphate dehydrogenase variant associated with undetectable enzyme activity and immunologically cross-reacting material. Am.J.Hum.Genet. 51:386-395, 1992. Notes: Among a large number of glucose-6-phosphate dehydrogenase (G6PD) variants associated with different severity of clinical manifestations, enzyme deficiency, and kinetic abnormalities

found in humans, only one variant exhibits no measurable activity and lacks an immunologically cross- reacting material in blood cells and other tissues. The mRNA content of the patient's lymphoblastoid cells was found to be normal, and the size of mRNA was also normal (i.e., alpha 24 kb). Western blot hybridization indicated that the patient's cells did not produce cross-reacting material. The variant mRNA was reverse transcribed and amplified by PCR. Nucleotide sequencing of the variant cDNA showed the existence of three nucleotide base changes, i.e., a C-->G at nucleotide 317 (counting from adenine of the initiation codon), which should cause Ser-->Cys substitution at the 106th position (counting from the initiation Met); a CAT at nucleotide 544, which induces the Arg-->Trp at the 182d position; and a C-->T at nucleot * Matsuoka, N. Phylogenetic relationships of echinoderms deduced from kinetic similarity of glucose-6-phosphate dehydrogenase. Comp.Biochem.Physiol. 103B:133-137, 1992. * Meloni, T., Pacifico, A., Forteleoni, G., and Meloni, G.F. G6PD deficiency and diabetes mellitus in northern Sardinian subjects. Haematologica 77:94-95, 1992. * Perng, L.-I., Chiou, S.-S., Liu, T.-C., and Chang, J.-G. A novel C to T substitution at nucleotide 1360 of cDNA which abolishes a natural Hha I site accounts for a new G6PD deficiency gene in Chinese. Hum.Mol.Genet. 1:205, 1992. * Phillippe, M., Larondelle, Y., Ursini, M.V., Martini, G., Corcoran, C.M., Mason, P.J., and Luzzatto, L. Functional characterization of the human glucose-6-phosphate dehydrogenase (G6PD) gene promoter. Blood 80 (Suppl 1):275a, 1992. * Pittalis, S., Martinez di Montemuros, F., Tavazzi, D., and Fiorelli, G. Rapid isolation of glucose-6-phosphate dehydrogenase from human erythrocytes by combined affinity and anion-exchange chromatography for biochemical characterization of variants. J.Chromatogr.Biomed.Appl. 573:29-34, 1992. Notes: A new method is presented for the purification of human glucose-6- phosphate dehydrogenase (G6PD) using affinity chromatography with 2'5'- ADP-Sepharose 4B followed by automated ion-exchange chromatography with DEAE 5PW. This rapid method allows a high recovery of enzyme activity from even a small amount of blood; the yield is about 90% after the first purification step and 70% at the end of the procedure There is an excellent reproducibility of the kinetic parameters and optimal biochemical characterization of G6PD is achieved even for variants associated with severe enzyme deficiency (e.g. G6PD Mediterranean). AUTHOR. * Prchal, J.T., Harmon, W.A., and Hirschowitz, B.I. Gilbert's syndrome associated with new variant of G6PD deficiency: G6PD-Pawnee. Unpublished , 1992. * Reeve, P.A., Toaliu, H., Kaneko, A., Hall, J.J., and Ganczakowski, M. Acute intravascular haemolysis in Vanuatu following a single dose of primaquine in individuals with glucose-6-phosphate dehydrogenase deficiency. J.Trop.Med.Hyg. 95:349-351, 1992. Notes: In 1989 and 1990 several patients were admitted to hospitals in Vanuatu with acute intravascular haemolysis following standard malaria treatment. This included a single 45-mg dose of primaquine given as a malaria control measure for its gametocytocidal effect. Seven of them (all those tested) were subsequently confirmed to have glucose-6-phosphate dehydrogenase (G6PD) deficiency, using a visual colorimetric test kit (Sigma Chemical Co. Ltd). The case reports of four patients admitted to

Vila Central Hospital and managed by one of us (PAR) are discussed in detail. AUTHOR. * Saad, S.T.O. and Costa, F.F. Glucose-6-phosphate dehydrogenase deficiency and sickle cell disease in Brazil. Hum.Hered. 42:125-128, 1992. Notes: The frequency of glucose-6-phosphate dehydrogenase (G-6PD) deficiency was determined in 54 male patients with sickle cell diseases: 31 sickle cell anemia (SS), 14 sickle cell hemoglobinopathyc (SC) and 9 HbS/beta- thalassemia (S/B- thal) by a combination of quantitative assay, fluorescent spot test and electrophoresis. Of the 54 patients tested, 7 were found to be G-6-PD deficient (G-6-PD-) (3 SS,3 SC and 1 S/B-thal) and 47 G-6-PD normal (G-6-PD+) (6 G-6-PD A and 41 G-6-PD B). All the deficient patients were G-6- PD A-. The frequency of G-6-PD deficiency did not differ significantly from that observed in the general population. Compared to patients who were not G-6-PD-, there were no significant differences in the hemoglobin concentration and reticulocyte count in patients with sickle cell diseases who were G-6-PD. AUTHOR. * Sayyed, Z., Mukherjee, M.B., Mudera, V.C., Colah, R., and Gupte, S. Characterization of G6PD Rohini--a new class III Indian variant. Indian J.Med.Res. 96:96-100, 1992. Notes: A new Indian G6PD variant was detected in a 15 yr old Maratha male during a population screening programme in high school children in Bombay (India). The propositus and two family members having the same variant were apparently healthy. This enzyme variant has a mild erythrocyte G6PD deficiency and a slow electrophoretic mobility. It is characterized by a high Michaelis-Menton constant for G6P, a bimodal curve for pH optima and a slight decrease in the thermostability. The rate of utilization of substrate analogue is similar to that of normal. These observations suggest identification of a new class III variant, designated as G6PD Rohini. * Scanlan, D.J., Newman, J., Sebaihia, M., Mann, N.H., and Carr, N.G. Cloning and sequence analysis of the glucose-6-phosphate dehydrogenase gene from the cyanobacterium Synechococcus PCC 7942. Plant Mol.Biol. 19:877-880, 1992. Notes: The glucose-6-phosphate dehydrogenase (EC 1.1.1.49) gene (zwf) of the cyanobacterium Synechococcus PCC 7942 was cloned on a 2.8 kb Hind III fragment. Sequence analysis revealed an ORF of 1572 nucleotides encoding a polypeptide of 524 amino acids which exhibited 41% identity with the glucose- 6-phosphate dehydrogenase of Escherichia coli. AUTHOR. * Severin, E. and Seidler, E. Calibration of a flow cytometric assay of glucose-6-phosphate dehydrogenase activity. Cytometry 13:322-326, 1992. Notes: The reduction of tetrazolium salts to colored formazans is a reaction which has been exploited both in histo- and cytochemistry. Tetrazolium salts forming fluorescent formazans prove suitable for measuring defined cellular dehydrogenase activities in automated processes. This study considers an important aspect of formazan measurement in flow cytometry, namely, calibration. Calibration is performed by correlating the number (and fluorescence intensity) of formazan-bearing cells measured by flow cytometry with simultaneously performed biochemical analyses of the same material. The method is demonstrated by an example of glucose-6-phosphate dehydrogenase. Using the data of a typical experiment, the enzyme activity is expressed in femtomol of hydrogen transferred per cell during incubation time. Furthermore, through spatially resolved double

excitation of formazan and nuclear DAPI fluorescence, an independent analysis of cell cycle and cellular enzymatic activity is established. AUTHOR. * Tagarelli, A., Cittadella, R., Bria, M., and Brancati, C. Glucose-6-phosphate dehydrogenase (G6PD) deficiency in the Albanian ethnic minority of Cosenza province, Italy. Gene Geography 6:71-78, 1992. * Tang, T.K., Tam, K.-B., and Huang, S.-C. High-level expression of a functional human G6PD enzyme in the erythroid cells of transgenic mice. Blood 80 (Suppl 1):275a, 1992. * Tang, T.K., Huang, C.-S., Huang, M.-J., Tam, K.-B., Yeh, C.-H., and Tang, C.-J.C. Diverse point mutations result in glucose-6-phosphate dehydrogenase (G6PD) polymorphism in Taiwan. Blood 79:2135-2140, 1992. Notes: Glucose-6-PHOSPHATE dehydrogenase (G6PD; EC 1.1.1.49) deficiency is the most common human enzymopathy, affecting more than 200 million people worldwide. Although greater than 400 variants have been described based on clinical and biochemical criteria, little is known about the molecular basis of these G6PD deficiencies. Recently, the gene that encodes human G6PD has been cloned and sequenced, which enables us to examine directly the heterogeneity of G6PD at the DNA level. During the past 10 years, we examined the G6PD activity in 21,271 newborn Chinese infants (11,400 males and 9,871 females) and identified 314 (2.8%) males and 246 (2.5%) females having low G6PD activity. The G6PD gene from 10 randomly selected affected individuals and their relatives was polymerase chain reaction (PCR) amplified, subcloned, and sequenced. Dur results indicate that at least four types of mutation are responsible for the G6PD polymorphism in Taiwan. The first type of mutation (487 G --> A) was found in an affected Ch * Thakur, A. and Verma, I.C. Interaction of malarial infection and glucose-6-phosphate dehydrogenase deficiency in Muria gonds of district Bastar, central India. Trop.Geogr.Med. 44:201-205, 1992. Notes: Muria gond tribals (n = 473) from district Bastar, central India, an area known to be hyperendemic for malaria, were investigated for malarial infection and glucose-6-phosphate dehydrogenase deficiency. The frequency of G-6-PD deficiency was 21.3% among male subjects and 3.7% among females. Assay of malarial antibodies showed that seropositivity as well as the level of antibodies was significantly higher in male subjects with normal enzyme levels as compared with males G-6-PD deficiency. Females with normal G-6-PD enzyme levels too had higher seropositivity as well as level of antibodies against malaria as compared with females having G-6-PD deficiency. This suggests that G-6-PD deficiency correlates with a higher degree of resistance. AUTHOR. * Town, M., Bautista, J.M., Mason, P.J., and Luzzatto, L. Both mutations in G6PD A- are necessary to produce the G6PD deficient phenotype. Hum.Mol.Genet. 1:171-174, 1992. * Tuttle, S.W., Varnes, M.E., Mitchell, J.B., and Biaglow, J.E. Sensitivity to chemical oxidants and radiation in CHO cell lines deficient in oxidative pentose cycle activity. Int.J.Radiat.Oncol.Biol.Phys. 22:671-675, 1992. Notes: In this paper we examine the susceptibility of a series of G6PD-CHO cell lines to a variety of chemical oxidants. Addition of these drugs to KID, the parental cell line, results in as much as a 20-fold increase in pentose cycle (PC) activity over control values. In two of our mutant lines, E16 and E48,

little or no stimulation of PC activity is seen. These lines are shown to be much more susceptible to the toxic effects of the chemical oxidants t-butyl hydroperoxide and diamide. PC activity is also stimulated by ionizing radiation in KID cells. One of the G6PD cell lines has an increased aerobic radiation response compared to the parental line. However, since this is not the case with the other G6PD- cell lines, it is unclear whether this represents a difference in the absolute value of PC activity or some additional variable that may be influencing the results. AUTHOR. * VandeBerg, J.L., Aivaliotis, M.J., and Samollow, P.B. X-linked glucose-6-phosphate dehydrogenase (G6PD) and autosomal 6-phosphogluconate dehydrogenase (6PGD) polymorphisms in baboons. Biochem.Genet. 30:567-580, 1992. Notes: Electrophoretic polymorphisms of glucose-6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase (6PGD) were examined in captive colonies of five subspecies of baboons (Papio hamadryas). Phenotype frequencies and family data verified the X-linked inheritance of the G6PD polymorphism. Insufficient family data were available to confirm autosomal inheritance of the 6PGD polymorphism, but the electrophoretic patterns of variant types (putative heterozygotes) suggested the codominant expression of alleles at an autosomal locus. Implications of the G6PD polymorphism are discussed with regard to its utility as a marker system for research on X- chromosome inactivation during baboon development and for studies of clonal cell proliferation and/or cell selection during the development of atherosclerotic lesions in the baboon model. AUTHOR. * Vulliamy, T., Mason, P., and Luzzatto, L. The molecular basis of glucose-6-phosphate dehydrogenase deficiency. Trends Genet. 8:138-143, 1992. Notes: With more than 300 different variants reported the human enzyme glucose- 6-phosphate dehydrogenase (G6PD; EC 1.1.1.49) is one of the most polymorphic proteins known. An estimated 400 million people throughout the world are deficient in G6PD; numerous lines of evidence indicate that this is because female heterozygotes have a selective advantage in malaria infections. The cloning of the G6PD gene has made it possible to clarify the molecular basis underlying this enzyme deficiency and polymorphism. AUTHOR. * Willems, P.J. and Vits, L. PCR detection of a BclI RFLP in the G6PD gene of Caucasians. Hum.Genet. 89:579, 1992. Notes: We have calculated the frequencies of two alleles of the glucose-6- phosphate dehydrogenase gene in a randomly selected group of Caucasians. Allele 1 has a frequency of 82%. whereas that of allele 2 is 18%. * Yu, M.-W., Hsiao, K.-J., Wuu, K.-D., and Chen, C.-J. Association between glucose-6-phosphate dehydrogenase deficiency and neonatal jaundice: Interaction with multiple risk factors. Int.J.Epidemiol. 21:947-952, 1992. Notes: This nonconcurrent cohort study was carried out to evaluate the association of neonatal jaundice with glucose-6-phosphate dehydrogenase (G-6-PD) deficiency and its interactions with other risk factors. The G-6-PD enzyme activity of 12379 neonates was screened by a semi-quantitative fluorometric assay and double-checked by a quantitative method to identify a G-6-PD deficient cohort of 333 neonates. Matched with these on birth date, sex and delivery hospital were a G6-PD normal cohort of 653 neonates. Neonatal jaundice was defined by a peak serum bilirubin (PSB) level of >/= 15 mg/ dl. A

significant association between G-6-PD deficiency and neonatal jaundice was observed in male but not female neonates. There was an inverse dose-response relation between G-6-PD activity and neonatal jaundice among male neonates. Both hypoxia /asphyxia and maternal hepatitis B surface antigen (HBsAg) carrier status were associated with an increased risk of neonatal jaundice among G-6-PD deficient but not G-6-PD norma * Assaf, A.A., Tabbara, K.F., and el-Hazmi, M.A. Cataracts in glucose-6-phosphate dehydrogenase deficiency. Ophthalmic Paediatr.Genet. 14:81-86, 1993. Notes: Glucose-6-phosphate dehydrogenase (G-6-PD) deficiency plays an important biochemical role in the metabolism of the lens. Controversies exist in the literature on the possible association between G-6-PD deficiency and the development of cataracts. The authors present ten patients, aged between infancy and 40 years of age, who were admitted for bilateral congenital or presenile cataracts. These patients had no ocular or systemic disease which might have caused their cataract. The only systemic finding they had was G-6-PD deficiency. Two other patients among the families described suffered from bilateral congenital or presenile cataracts with no G-6-PD deficiency. This deficiency state does not appear to play a role in the production of their cataracts. * Baronciani, L., Tricta, F., and Beutler, E. G6PD "Campinas:" A deficient enzyme with a mutation at the far 3' end of the gene. Hum.Mutat. 2:77-78, 1993. Notes: (MS377) (B959). * Beutler, E. The study of glucose-6-dehydrogenase: History and molecular biology. Am.J.Hematol. 42:53-58, 1993. Notes: (MS333) (B944). * Beutler, E. Comment on "Study of glucose-6-phosphate dehydrogenase: History and molecular biology," by Ernest Beutler, Am J Hematol 42:53-58, 1993. Reply. Am.J.Hematol. 44:216, 1993. * Beutler, E. The molecular biology of enzymes of erythrocyte metabolism. In: The Molecular Basis of Blood Diseases, edited by Stamatoyannopoulos, G., Nienhuis, A.W., Majerus, P.W., and Varmus, H.Philadelphia:W.B.Saunders Co. 1993,p. 331-349. Notes: (MS297). * Brewer, G.J. Comment on "Study of glucose-6-phosphate dehydrogenase: History and molecular biology," by Ernest Beutler, Am J Hematol 42:53-58, 1993. Am.J.Hematol. 44:215-216, 1993. * Calabro, V., Mason, P.J., Filosa, S., Civitelli, D., Cittadella, R., Tagarelli, A., Martini, G., Brancati, C., and Luzzatto, L. Genetic heterogeneity of glucose-6-phosphate dehydrogenase deficiency revealed by single-strand conformation and sequence analysis. Am.J.Hum.Genet. 52:527-536, 1993. Notes: We have carried out a systematic study of the molecular basis of glucose-6-phosphate dehydrogenase (G6PD) deficiency on a sample of 53 male subjects from Calabria, in southern Italy. Our sequential approach consisted of the following steps: (1) Partial biochemical characterization was used to pinpoint candidate known variants. The identity of these was then verified by restriction-enzyme or allele- specific oligonucleotide hybridization analysis of the appropriate PCR-amplified fragment. (2) On samples for which there was no obvious candidate mutation, we proceeded to amplify the entire coding region in eight fragments, followed by single- strand conformation polymorphism (SSCP) analysis of each fragment. (3) The next step was M13 phage cloning and sequencing of those individual fragments that were found to be abnormal by SSCP. Through this approach we have

identified the molecular lesion in 51 of the 53 samples. In these we found a total of nine different G6PD- deficient variants, five of which (G6 * Cappellini, M.D., Tavazzi, D., Martinez di Montemuros, F., Sampietro, M., Gaviraghi, A., Carandini, D., and Fiorelli, G. Alternative splicing of human G6PD messenger RNA in K562 cells but not in cultured erythroblasts. Eur.J.Clin.Invest. 23:188-191, 1993. Notes: The biochemical properties of glucose-6-phosphate dehydrogenase (G6PD) vary in different tissues, and different protein isoforms of the enzyme have been described. Alternative splicing of G6PD intron VII has been detected in transformed lymphoblasts, granulocytes and spermatocytes; the function of this mRNA species is still unknown. We developed a PCR for detecting alternatively spliced G6PD mRNA in K562 and in erythroblasts at different stage of maturation obtained from human peripheral BFU-E in order to evaluate a possible physiological role during erythroid maturation. Trace events of alternative splicing of G6PD intron VII sequences were observed in K562 cells but not in BFU-E-derived erythroid precursors; we consider this phenomenon a non-functional activity in the cells analysed. AUTHOR. * Chiu, D.T.Y., Zuo, L., Chao, L., Chen, E., Louie, E., Lubin, B., Liu, T.Z., and Du, C.S. Molecular characterization of glucose-6-phosphate dehydrogenase (G6PD) deficiency in patients of Chinese descent and identification of new base substitutions in the human G6PD gene. Blood 81:2150-2154, 1993. * Filosa, S., Calabro, V., Lania, G., Vulliamy, T.J., Brancati, C., Tagarelli, A., Luzzatto, L., and Martini, G. G6PD haplotypes spanning Xq28 from F8C to red/green color vision. Genomics 17:6-14, 1993. * Gorlin, J.B., Henske, E., Warren, S.T., Kunst, C.B., D'Urso, M., Palmieri, G., Hartwig, J.H., Bruns, G., and Kwiatkowski, D.J. Actin-binding protein (ABP-280) filamin gene (FLN) maps telomeric to the color vision locus (R/GCP) and centromeric to G6PD in Xq28. Genomics 17:496-498, 1993. Notes: * We have mapped the ABP-280 filamin gene (FLN) to Xq28 by Southern blot analysis of somatic cell hybrid lines, by fluorescence in situ hybridization, and through identification of portions of the FLN gene within cosmids and YACs mapped to Xq28. The FLN gene is found within a 200-kb region centromeric to the G6PD locus and telomeric to DSX52 and the color vision locus. * Greene, L.S. G6PD deficiency as protection against falciparum malaria: An epidemiologic critique of population and experimental studies. Yearbook of Physical Anthropology 36 Suppl. 17:153-178, 1993. * Greene, L.S., McMahon, L., and DiIorio, J. Co-evolution of glucose-6-phosphate dehydrogenase deficiency and quinine taste sensitivity. Ann.Hum.Biol. 20:497-500, 1993. Notes: We hypothesized that 'quinine' taste sensitivity functions to regulate the intake of bitter-tasting, naturally occurring antimalarial substances of plant origin, and that this genetic trait has co-evolved with the G6PD locus. This hypothesis was tested by evaluating taste sensitivity to quinine sulphate and sodium chloride among 17 G6PD-deficient and 25 G6PD-normal African American subjects 14-40 years of age. There was no significant difference in mean 'quinine' taste sensitivity between the two groups, although there was a trend towards greater 'quinine' taste acuity among the G6PD-deficient subjects.

A larger study sample would provide a fairer test of the hypothesis. * Hirono, A., Fujii, H., Shima, M., and Miwa, S. G6PD Nara: A new class 1 glucose-6-phosphate dehydrogenase variant with an eight amino acid deletion. Blood 82:3250-3252, 1993. * Hirono, A., Fujii, H., and Miwa, S. Molecular abnormality of G6PD Konan and G6PD Ube, the most common glucose-6-phosphate dehydrogenase variants in Japan. Hum.Genet. 91:507-508, 1993. Notes: G6PD Konan and G6PD Ube are the most common glucose-6-phosphate dehydrogenase (G6PD) variants found in Japan. To clarify the molecular abnormality of these two variants, the entire coding region was amplified by polymerase chain reaction from genomic DNA (G6PD Konan) or cDNA (G6PD Ube). Direct sequencing revealed that both variants have the same nucleotide substitution (241 C to T) in exon 4, which predicts an Arg to Cys substitution at amino acid 81. * Hsia, Y.E., Miyakawa, F., Baltazar, J., Ching, N.S.P., Yuen, J., Westwood, B., and Beutler, E. Frequency of glucose-6-phosphate dehydrogenase (G6PD) mutations in Chinese, Filipinos, and Laotians from Hawaii. Hum.Genet. 92:470-476, 1993. Notes: (MS379) (B981)In a Hawaii Hereditary Anemia Screening Project, 4,984 participants were tested for glucose-6-phosphate dehydrogenase (G6PD) deficiency by a filter paper blood spot fluorescence test. Abnormal samples and suspected heterozygotes were checked by quantitative G6PD assay (normal 4.5 to 14 units/g Hb). G6PD was deficient (<1.5 units/g Hb) in 188 of 2,155 males; 7 other males had low activity (1.5 to 2.8 units/g Hb). The gene frequency, estimated from males after excluding referred and related cases, was 0.037 for Chinese, 0.134 for Filipinos, and 0.203 for Laotians. Among 2,829 females tested, family data showed 111 females were obliged to be at least heterozygous, regardless of G6PD activity, and 43 others had low G6PD activity. Most heterozygotes probably remained undetected by G6PD screening. In 28 females, activity was under 10%; in another 9 females, activity was <1.5 units/g Hb. Since only 25 homozygotes would be predicted, this apparent excess of females with deficient activity coul * Irshaid, Y.M., Al-Hadidi, H.F., and Rawashdeh, N.M. Lack of association between glucose-6-phosphate dehydrogenase deficiency and dextromethorphan O-demethylation polymorphism. Eur.J.Clin.Pharmacol. 44:303-304, 1993. * Jeffery, J., Persson, B., Wood, I., Bergman, T., Jeffery, R., and Jrnvall, H. Glucose-6-phosphate dehydrogenase--Structure-function relationships and the Pichia jadinii enzyme structure. Eur.J.Biochem. 212:41-49, 1993. Notes: The primary structure of glucose-6-phosphate dehydrogenase from the yeast Pichia jadinii (formerly Candida utilis) has been determined. It consists of a 495-residue, N-terminally acetylated protein chain. The structure shows extensive differences from those of the corresponding mammalian, fruit fly, and bacterial enzymes (52-68% residue non-identities), but also from that of another yeast. Saccharomyces cerevisiae (38%). A eubacterial type and a yeast type of glucose-6- phosphate dehydrogenase are discerned, in addition to the known mammalian type. They are distinguished from each other, from the mammalian type, and the insect enzyme, on the basis of both specific residues and pattern differences. The distribution of residues conserved in all forms locates short segments in which identities are closely grouped. Approximately 50% of these segments correspond to predicted turns and appear to mark the principal folds characteristic of the

enzyme's tertiary structure. A region in the N- terminal part of * Kanno, H., Kondoh, T., and Yoshida, A. 5' structure and expression of human glucose-6-phosphate dehydrogenase mRNA. DNA Cell Biol. 12:209-215, 1993. Notes: The human glucose-phosphate (G6PD) cDNAs cloned from normal and carcinoma cells can encode 545-amino-acid residues starting from the first in-frame chain initiation codon. However, it was reported that the G6PD mRNAs of carcinoma cell lines were shorter and could encode only 515- amino-acid residues (Martini et al., 1986). We demonstrated the existence of two major G6PD mRNAs in normal reticulocytes, lymphoblasts, and hepatocytes by the primer extension analysis. The longer mRNA has a cap site at approx. nucleotide -166 and can encode 545-amino-acid residues, whereas the shorter mRNA has a cap site at approx. nucleotide -66, and encodes 515-amino-acid residues. These two naturally existing mRNAs (cDNAs) and an artificially truncated mRNA, which can encode the carboxy- terminal 479-amino-acid residues of the subunit, were expressed in the in vitro reticulocyte and wheat germ systems and in the in vivo E. coli system. All three species of mRNA (cDNA) were efficiently translated and produced proteins w * Martins, M.C., Olim, G., Melo, J., Magalhaes, H.A., and Rodrigues, M.O. Hereditary anaemias in Portugal: Epidemiology, public health significance, and control. J.Med.Genet. 30:235-239, 1993. Notes: A countrywide prospective study aimed at establishing the prevalence of the haemoglobinopathy genes in the Portuguese population was carried out by screening 15208 randomly selected blood samples from young males. This male based survey provided the opportunity of assessing simultaneously the prevalence of the red cell enzyme glucose-6-phosphate dehydrogenase (G6PD) deficiency, thus giving a picture of these important hereditary anaemias in Portugal. The results showed a low average frequency of beta thalassaemia (0.45%) and haemoglobin S (0.32%) carriers as well as G6PD deficiency (0.51%). However, these disorders are unevenly distributed throughout the country with a higher prevalence in some areas, mainly in the south. The relationship of this pattern of haemoglobinopathies to the known haplotypes linked to beta thalassaemia and sickle cell disease, relevant historical events, and local selective pressure was investigated. Hb D and Hb J are the commonest other structural variants. The implemented * Meola, G., Tremblay, J.P., Sansone, V., Rotondo, G., Radice, S., Bresolin, N., Huard, J., and Scarlato, G. Muscle glucose-6-phosphate dehydrogenase deficiency: Restoration of enzymatic activity in hybrid myotubes. Muscle Nerve 16:594-600, 1993. Notes: A high level of glucose-6-phosphate dehydrogenase (G6PD) activity was observed in myoblasts and myotubes from normal human and mouse cell cultures. However, only a residual amount of activity was observed in myoblasts and myotubes obtained from G6PD-deficient patients (G6PD Mediterranean). Hybrids were formed by the fusion of normal (from human and mouse) and G6PD-deficient myoblasts (from the patients). These hybrids contained a high level of G6PD activity. Hoechst staining permitted to confirm that the enzymatic activity was not restrained to a domain near the competent nuclei. These results suggest that myoblast transplantation could be used to restore normal enzymatic activity in metabolic myopathies. * Micheli, V., Simmonds, H.A., Bari, M., and Pompucci, G.

HPLC determination of oxidized and reduced pyridine coenzymes in human erythrocytes. Clin.Chim.Acta 220:1-17, 1993. * Muggeo, M., Moghetti, P., Querena, M., Cacciatori, V., Zoppini, G., Zenere, M., Tosi, F., Travia, D., and Bonora, E. Mononuclear leukocytes from obese patients with type II diabetes have reduced activity of hexokinase, 6-phosphofructokinase and glucose-6-phosphate dehydrogenase. Horm.Metab.Res. 25:160-164, 1993. Notes: In the present study we measured the activity of some cytosolic enzymes involved in intracellular glucose metabolism in mononuclear leukocytes from 77 obese subjects of which 39 were nondiabetic and 38 had newly- diagnosed untreated type II diabetes mellitus. 28 subjects (19 nondiabetic and 18 diabetic) had also a study of insulin binding to monocytes. 35 subjects (14 nondiabetic, 21 diabetic) underwent an insulin tolerance test for the evaluation of in vivo insulin action. Mononuclear leukocytes from diabetic obese patients showed significantly lower activities of hexokinase (HK), 6-phosphofructokinase (PFK) and glucose-6-phosphate dehydrogenase (G6PDH), while pyruvate kinase (PK) and 6-phosphogluconate dehydrogenase (6PGDH) activities were similar in the two groups. In the whole population HK and G6PDH activities inversely correlated with fasting and 2-h OGTT plasma glucose levels. Neither plasma insulin levels nor maximal specific insulin binding to monocytes were significantly correlated with an * Ninfali, P., Baronciani, L., Ruzzo, A., Fortini, C., Amadori, E., Dall'ara, G., Magnani, M., and Beutler, E. Molecular analysis of G6PD variants in northern Italy: A study on the population from the Ferrara district. Hum.Genet. 92:139-142, 1993. Notes: (MS382)(B969) In the Ferrara district, an area south of the Po delta, four different variants of glucose-6-phosphate dehydrogenase (G6PD; E.C.1.1.49) have been described as a result of biochemical characterization of the enzyme protein: one was G6PD Mediterranean (G6PD Med) and three were local variants named Ferrara I, II, and III. The Ferrara I variant was recently analysed at the DNA level and shown to correspond to G6PD A376G/202A, while the mutations causing the variants II and III, still remain unknown. We analysed the G6PD coding region of 18 apparently unrelated G6PD deficient subjects, whose families have lived in the Ferrara district for at least three generations: 12 subjects had G6PD Med563T/1311T, 3, G6PD Santamaria376G/542T and 2, G6PD A-376G/202A. In one subject we found a new mutation, a G - > A transition at nucleotide 242 causing an Arg -> His amino-acid replacement at position 81. We named this new variant G6PD Lagosanto242 A. Phenotypically the enzyme has nearly normal kinetic pr * Nonneman, D., Stockham, S.L., Shibuya, H., Messer, N.T.I., and Johnson, G.S. A missense mutation in the glucose-6-phosphate dehydrogenase gene associated with hemolytic anemia in an American saddlebred horse. Blood 82 (Suppl 1):466a, 1993. * Oblender, M. Index of suspicion. Case 3. Kernicterus in a baby girl homozygous for glucose-6-phosphate dehydrogenase deficiency. Pediatr.Rev. 14:191, 193, 1993. * Oppenheim, A., Jury, C.L., Rund, D., Vulliamy, T.J., and Luzzatto, L. G6PD Mediterranean accounts for the high prevalence of G6PD deficiency in Kurdish Jews. Hum.Genet. 91:293-294, 1993. Notes: The Jews of Kurdistan are a small inbred population with a high incidence of beta-thalassaemia and glucose-6-phosphate dehydrogenase (G6PD) deficiency. Recently, it was reported that

the beta-thalassaemia in this population shows an unusual mutational diversity: 13 different mutations were identified, of which 4 had not previously been observed in any other population. In contrast, we now report that the G6PD deficiency, which has the highest known incidence in the world, and which affects about 70% of males, is almost entirely attributable to a single widespread mutation, G6PD Mediterranean. AUTHOR. * Paglia, D.E. Acute episodic hemolysis in the African black rhinoceros as an analogue of human glucose-6-phosphate dehydrogenase deficiency. Am.J.Hematol. 42:36-45, 1993. Notes: Sudden episodes of massive hemolysis have become the most common cause of death among captive black rhinoceroses, and there is evidence that they occur in the wild as well. We have observed radically unique enzyme and metabolite profiles in normal rhinoceros erythrocytes compared to humans and other mammals, including marked deficiencies of intracellular adenosine triphosphate (ATP), catalase, adenosine deaminase, and other enzymes involved in glycolysis, glutathione cycling, and nucleotide metabolism. Minimal concentrations of ATP appear to impair effective acceleration of hexosemono-phosphate shunt activity in response to oxidants by restricting substrate generation at the hexokinase step. Antioxidant defenses are further compromised by catalase deficiency, which may be a general characteristic of rhinoceros erythrocytes, perhaps related to the common occurrence of severe mucocutaneous ulcerative disease. It is proposed that erythrocyte ATP deficiency in rhinoceroses may be an evolutionary adaptat * Ragusa, R., Di Cataldo, A., Gangarossa, S., Lo Nigro, L., and Schiliro, G. Low-grade haemolysis and assessment of iron status during the steady state in G6PD-deficient subjects. Acta Haematol.(Basel) 90:25-28, 1993. * Rais, N., Churi, C., Shah, A., and Kapoor, A. Glucotoxicity and oxidative hemolysis in G-6-PD deficiency. Diabetes Care 16:1215-1216, 1993. * Rees, D.C., Kelsey, H., and Richards, J.D.M. Lesson of the Week: Acute haemolysis induced by high dose ascorbic acid in glucose-6-phosphate dehydrogenase deficiency. BMJ 306:841-842, 1993. * Ruzzo, A., Ninfali, P., and Magnani, M. Glucose-6-phosphate dehydrogenase nucleotide 1311 polymorphism in Central Italy (Marche region). Enzyme Protein 47:22-26, 1993. * Scott, M.D., Wagner, T.C., and Chiu, D.T.-Y. Decreased catalase activity is the underlying mechanism of oxidant susceptibility in glucose-6-phosphate dehydrogenase-deficient erythrocytes. Biochim.Biophys.Acta 1181:163-168, 1993. Notes: Historically, it has been theorized that the enhanced oxidant sensitivity of glucose-6-phosphate dehydrogenase (G6PD)-deficient erythrocytes arises as a direct consequence of an inability to maintain cellular glutathione (GSH) levels. This study alternatively hypothesizes that decreased NADPH concentration leads to impaired catalase activity which, in turn, underlies the observed oxidant susceptibility. To investigate this hypothesis, normal and G6PD-deficient erythrocytes and hemolysates were challenged with a H2O2- generating agent. The results of this study demonstrated that catalase activity was severely impaired upon H2O2 challenge in the G6PD- deficient cell while only a transient decrease was observed in normal cells. Supplementation of either normal or G6PD-deficient hemolysates with purified NADPH was found to significantly (P< 0.001) inhibit catalase inactivation upon oxidant challenge while addition of

NADP+ had no effect. Analysis of these results demonstrated direct correlation between * Sedlacek, Z., Korn, B., Konecki, D.S., Siebenhaar, R., Coy, J.F., Kioschis, P., and Poustka, A. Construction of a transcription map of a 300 kb region around the human G6PD locus by direct cDNA selection. Hum.Mol.Genet. 2:1865-1869, 1993. * Shalev, O., Bogomolski-Yahalom, V., and Sharon, R. Hemolysis following transfusion of erythrocytes from a donor with G6PD deficiency and a-thalassemia minor. Isr.J.Med.Sci. 29:214-216, 1993. * Shalev, O., Manny, N., and Sharon, R. Posttransfusional hemolysis in recipients of glucose-6-phosphate dehydrogenase-deficient erythrocytes. Vox Sang. 64:94-98, 1993. Notes: To test the hypothesis that transfusion of blood donated by individuals with glucose-6-phosphate dehydrogenease (G6PD) deficiency may result in a hemolytic reaction, we conducted a prospective longitudinal study in which 10 patients transfused with 1 unit of G6PD-deficient and 1 unit of normal red blood cells (RBC) were compared with 10 patients transfused with 2 units of age-matched normal RBC. We found that 24 h after transfusion serum bilirubin (umol/l) in the recipients of G6PD-deficient RBC was significantly higher than in the recipients of normal RBC (36 +/- 14 vs. 18 +/- 5, respectively, p> 0.004). A parallel increase was found in the serum lactate dehydrogenase (LDH; IU/l) between the two groups (378 +/- 151 vs. 264 +/- 56, p< 0.001). The difference in serum bilirubin (26 +/10 vs. 15 +/-5, p< 0.03) was still noted 48 h after transfusion, with only a marginal difference (p< 0.08) in LDH. We conclude that an immediate posttransfusional hemolytic reaction can occur in recipients of G6PD- defi * Szweda, L.I., Uchida, K., Tsai, L., and Stadtman, E.R. Inactivation of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal. Selective modification of an active-site lysine. J.Biol.Chem. 268:3342-3347, 1993. Notes: Incubation of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides with 4-hydroxy-2- nonenal (HNE) results in a pseudo first- order loss of enzyme activity. The pH dependence of the inactivation rate exhibits an inflection around pH 10, and the enzyme is protected from inactivation by glucose 6-phosphate. Loss of enzyme activity corresponds with the formation of one carbonyl function per enzyme subunit and the appearance of a lysine-HNE adduct. The data presented in this paper are consistent with the view that the epsilon- amino group of a lysine residue in the glucose 6-phosphate- binding site reacts with the double bond (C3) of HNE, resulting in the formation of a stable secondary amine derivative and loss of enzyme activity. We have described a mechanism by which HNE may, in part, mediate free radical damage. In addition, a method for the detection of the lysine-HNE adduct is introduced. AUTHOR. * Tan, K.L. and Boey, K.W. Efficacy of phototherapy in neonatal hyperbilirubinaemia associated with glucose-6-phosphate dehydrogenase deficient status. Eur.J.Pediatr. 152:601-604, 1993. Notes: The efficacy of phototherapy in a group of 427 infants with hyperbilirubinaemia associated with glucose-6-phosphate dehydrogenase (G6PD) deficiency and a comparable group of 3924 G6PD normal infants with non-haemolytic hyperbilirubinaemia was evaluated. Phototherapy was highly effective in reducing bilirubin levels in both groups of infants, being significantly more effective in the group with normal G6PD status. Failure rate was very low (2.03/1000) in the group with normal G6PD status and

nil in the G6PD deficient group. Bilirubin rebound after phototherapy was unremarkable with very few infants requiring a second exposure - 4.68/1000 in the G6PD deficient group and 6.37/1000 in the G6PD normal group. All the babies tolerated photo-therapy well. Phototherapy would therefore seem to be a simple and effective method for the management of severe jaundice associated with G6PD deficiency. AUTHOR. * Tang, T.K., Tam, K.-B., and Huang, S.-C. High-level and erythroid-specific expression of human glucose- 6-phosphate dehydrogenase in transgenic mice. J.Biol.Chem. 268:9522-9525, 1993. Notes: Human Glc-6-P dehydrogenase (Glc-6-P) cDNA spanning the entire coding region was subcloned into a pSG5 vector that contains an early SV40 promoter. intron II of the rabbit beta-globin gene, and a polyadenylation signal. This expression cassette was then placed downstream of the human beta-globin locus control region and injected into fertilized mouse eggs. Among five transgenic founders that contained intact copies of the construct, one founder expressed human Glc- 6-P dehydrogenase enzyme in a high-level and erythroidspecific fashion (5 x higher than endogenous Glc-6- P dehydrogenase activity). When this male founder mated with a normal individual, all the offspring that carried the transgene showed high- level expression of Glc-6-P dehydrogenase activity in erythroid cells. The endogenous mouse Glc-6-P dehydrogenase in all high- expression mice could be competed out by forming a hybrid with human Glc-6-P dehydrogenase. Our results indicate that the locus control region can drive the human Glc-6-P * Vulliamy, T., Beutler, E., and Luzzatto, L. Variants of glucose-6-phosphate dehydrogenase are due to missense mutations spread throughout the coding region of the gene. Hum.Mutat. 2:159-167, 1993. Notes: (MS384)(B964). * Weimer, T.A., Salzano, F.M., Westwood, B., and Beutler, E. Molecular characterization of glucose-6-phosphate dehydrogenase (G6PD) variants from Brazil. Hum.Biol. 65:41-47, 1993. Notes: (MS350) (B953) G6PD Sao Borja. * Alfinito, F., Calabro, V., Cappellini, M.D., Fiorelli, G., Filosa, S., Iolascon, A., Miraglia del Giudice, E., Perrotta, S., Migliorati, R., Vallone, D., Rotoli, B., and Luzzatto, L. Glucose 6-phosphate dehydrogenase deficiency and red cell membrane defects: Additive or synergistic interaction in producing chronic haemolytic anaemia. Br.J.Haematol. 87:148-152, 1994. Notes: We have investigated two unrelated patients with congenital haemolytic anaemia in both of whom we found a combination of hereditary spherocytosis (HS) and glucose-6-phosphate dehydrogenase (G6PD) deficiency. Segregation of the two defects was documented in both families, who had different molecular abnormalities for both HS and G6PD deficiency. In one family the propositus had a reduced level of spectrin and G6PD Seattle (282Asp-->His). In the other family the propositus had a band 3 abnormality and was heterozygous for G6PD Mediterranean (188Ser-->Phe). From a comparison of clinical and haematological findings in family members with either or both abnormalities we conclude that in one case the two defects exhibited a synergistic effect, resulting in a severe chronic haemolytic anaemia; whereas in the other the association was simply additive. * Arese, P., Cappadoro, M., Giribaldi, G., and Turrini, F. The malaria/G6PD hypothesis revisited: Reply. Parasitol.Today

10:262-263, 1994. * Arruda, V.R., Saad, S.T.O., and Costa, F.F. Hairy-cell leukemia and glucose-6-phosphate dehydrogenase. Acta Oncol. 33:574, 1994. * Beutler, E. G6PD deficiency. Blood 84:3613-3636, 1994. Notes: (MS410) (B999). * Cai, W., Filosa, S., and Martini, G. DNA haplotypes in the G6PD gene cluster studied in the Chinese Li population and their relationship to G6PDCanton. Hum.Hered. 44:279-286, 1994. * Cappellini, M.D., Sampietro, M., Toniolo, D., Carandina, G., Martinez di Montemuros, F., Tavazzi, D., and Fiorelli, G. G6PD Ferrara I has the same two mutations as G6PD A(-) but a distinct biochemical phenotype. Hum.Genet. 93:139-142, 1994. Notes: The cloning and sequencing of the normal glucose-6-phosphate dehydrogenase (G6PD) gene has led to the study of the molecular defects that determine enzymatic variants. In this paper, we describe the mutations responsible for the Ferrara I variant in an Italian man with a family history of favism, from the Po delta. Nucleotide sequencing of this variant showed a G --> A mutation at nucleotide 202 in exon IV causing a Val --> Met amino acid exchange, and a second A --> G mutation at nucleotide 376 in exon V causing an Asn --> Asp amino acid substitution. Although on the basis of its biochemical properties this variant was classified as G6PD Ferrara I, it has the same two mutations as G6PD A(-), which is common in American and African blacks, and as the sporadic Italian G6PD Matera. The mutation at nucleotide 202 was confirmed by NlaIII digestion of a polymerase chain reaction amplified DNA fragment spanning 109bp of exon IV. The 109-bp mutated amplified sequence is not distinguishable from the normal * Cappellini, M.D., Sampietro, M., Toniolo, D., Carandina, G., Pittalis, S., Martinez di Montemuros, F., Tavazzi, D., and Fiorelli, G. Biochemical and molecular characterization of a new sporadic glucose-6-phosphate dehydrogenase variant described in Italy: G6PD Modena. Br.J.Haematol. 87:209-211, 1994. Notes: A new glucose-6-phosphate dehydrogenase variant detected in an Italian man from the Po delta is described and designated as G6PD Modena. Biochemical characterization of the variant enzyme revealed an activity 21% of normal, a slow electrophoretic mobility, increased K-m value for NADP, decreased K-m value for G6P and a complete absence of NADPH inhibition, which could account for the apparently nonhaemolytic feature of this variant. The cloning and sequencing of the G6PD Modena allele showed a G --> C transition at nucleotide 844 in exon VIII causing a Asp --> His amino acid substitution. On the basis of biochemical characterization, G6PD Modena is classified as a genuine variant but it has the same mutation as G6PD Seattle-like. * Cappellini, M.D., Di Montemuros, F.M., Dotti, C., Tavazzi, D., De Bellis, G., Debernardi, S., and Fiorelli, G. Molecular heterogeneity of glucose-6-phosphate dehydrogenase (G6PD) Mediterranean type in Italy. Blood 84:114a, 1994. * Cappellini, M.D., Martinez di Montemuros, F., and Fiorelli, G. Different origin of nt 1246 glucose-6-phosphate dehydrogenase mutation. Blood 84:3592, 1994. * Di Montemuros, F.M., Cappellini, M.D., Tavazzi, D., De Bellis, G., Debernardi, S., and Fiorelli, G. Molecular characterisation of an Italian G6PD variant responsible for chronic non-spherocytic haemolytic anaemia. Clin.Genet. 46:357-359, 1994. * El-Hazmi, M.A.F., Warsy, A.S., Bahakim, H.H., and

Al-Swailem, A. Glucose-6-phosphate dehydrogenase deficiency and the sickle cell gene in Makkah, Saudi Arabia. J.Trop.Pediatr. 40:12-16, 1994. Notes: This study was conducted on 689 Saudi males and females living in the Makkah area in the western province of Saudi Arabia. The frequency of severe glucose-6-phosphate dehydrogenase (G-6-PD) deficiency in the male and female populations was 0.055 and 0.042 respectively. The normal G-6-PD was G-6- PD-B+ and the G-6-PD phenotypes identified included G- PD- A+, G-6-PD-A-, G-6-PD-Mediterranean, and G-6-PD-Mediterranean- like at gene frequencies of 0.0288, 0.0026, 0.05497, and 0.1969 in the male population and 0.026, 0.0146, 0.0407, and 0.02606 in the female population. The main variants producing severe and mild G-6-PD deficiency were G-6-PD- Mediterranean and G-6-PD-Mediterranean-like, respectively. The sickle cell gene was identified at a frequency of 0.029 and no interaction between sickle cell and G-6-PD deficiency genes was encountered. AUTHOR. * Filosa, S., Cai, W., Galanello, R., Cao, A., De Mattia, D., Schettini, F., and Martini, G. A novel single-base mutation in the glucose 6-phosphate dehydrogenase gene is associated with chronic non-spherocytic haemolytic anaemia. Hum.Genet. 94:560-562, 1994. Notes: More then 80 variants of glucose-6-phosphate dehydrogenase (G6PD) are associated with chronic nonspherocytic haemolytic anaemia (CNSHA); however, the molecular basis of this association is not fully understood. We have used the polymerase chain reaction and nucleotide sequence analysis to characterize a new G6PD variant, which we designate as G6PD Bari, in a G6PD-deficientt boy affected by CNSHA. A single mutation leading to an amino-acid substitution was detected in the GGPD coding region, viz. a C-->T transition at position 1187 predicting leucine at residue 396 in the enzyme; proline is invariably present in evolutionary distant G6PD molecules at this position. Inheritance in the patient's family was demonstrated by the polymerase chain reaction followed by diagnostic restriction enzyme analysis. The C-->T transition responsible for GGPD Bari maps close to several other mutations previously identified in GGPD variants associated with CNSHA. * Fiorelli, G. and Cappellini, M.D. Unpublished , 1994. Notes: 1052T; 1342G. Both named Cagliari. * Forni, G.L., Napoli, G., Gaetani, G.F., and Ferraris, A.M. G6PD deficiency-related chronic hemolysis treated with splenectomy: A case report. Am.J.Hematol. 47:146-147, 1994. * Frigerio, R., Sole, G., Lovicu, M., and Passiu, G. Molecular and biochemical data on some glucose-6-phosphate dehydrogenase variants from Southern Sardinia. Haematologica 79:319-321, 1994. Notes: Background. Glucose-6-phosphate dehydrogenase (G6PD; E.C.1.1.1.49) deficiency is the most common human enzymopathy; nearly 400 different biochemical variants of the enzyme have been described. Sardinia is the Italian region with the highest frequency of this defect. Methods. We examined genomic DNA of 16 subjects with G6PD Mediterranean, 2 with G6PD Athens- like, 1 with G6PD Ferrara 2 (all as biochemically defined). Results. All G6PD Mediterranean subjects had a C-->T mutation at nudeotide 563 and a C-->T transition at nucleotide 1311; G6PD Athens-like and Ferrara 2 subjects had a G-->C mutation at nucleotide 844 (the same mutation has been found in G6PD Seattle-like). Conclusions. This study suggests that in Southern Sardinia G6PD mutations are relatively homogeneous and that the results of biochemical

characterization studies must be carefully evaluated, because the same mutations might be responsible for different biochemical behavior. * Friguet, B., Szweda, L.I., and Stadtman, E.R. Susceptibility of glucose-6-phosphate dehydrogenase modified by 4-hydroxy-2-nonenal and metal-catalyzed oxidation to proteolysis by the multicatalytic protease. Arch.Biochem.Biophys. 311:168-173, 1994. Notes: Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides is inactivated when exposed to metal-catalyzed oxidation or when modified by the lipid peroxidation product, 4-hydroxy- 2-nonenal (HNE). Although in each case inactivation appears to be the result of the selective modification of an active site lysine residue, only the oxidized enzyme becomes more susceptible to proteolysis by purified rat liver multicatalytic protease, a multienzymatic proteolytic complex involved in the intracellular degradation of damaged proteins. The HNE-treated enzyme remains as resistant to proteolysis by the multicatalytic protease as the native enzyme. In contrast to the HNE-treated Glu-6-PDH, enzyme modified by Fe2+ and citrate is more thermolabile and exhibits increased binding of the hydrophobic probe 8-anilino-1-naphtalene sulfonic acid (ANSA). Heat inactivation is characterized, in part, by dissociation of the dimer to inactive subunits. No change in the secondary structure and only small variations in th * Ganea, E. and Harding, J.J. Inactivation of glucose-6-phosphate dehydrogenase by glycation. Biochem.Soc.Trans. 22:445S, 1994. * Gerr, F., Frumkin, H., and Hodgins, P. Hemolytic anemia following succimer administration in a glucose-6-phosphate dehydrogenase deficient patient. J.Toxicol.Clin.Toxicol. 32:569-575, 1994. Notes: Because of its favorable side effects profile, the oral chelating agent dimercaptosuccinic acid is often used for treatment of lead intoxication. We report a case of a 45year-old black male with glucose-6-phosphate dehydrogenase deficiency and a 17 year history of occupational lead exposure who developed hemolysis during treatment with dimercaptosuccinic acid for symptomatic lead intoxication. * Hirono, A., Nakayama, S., Fujii, H., and Miwa, S. Molecular abnormality of a unique Japanese glucose-6-phosphate dehydrogenase variant (G6PD Kobe) with a greatly increased affinity for galactose-6-phosphate. Am.J.Hematol. 45:185-186, 1994. Notes: Systematic molecular analysis of a Japanese class 1 glucose- 6-phosphate dehydrogenase (G6PD) variant (G6PD Kobe) cDNA revealed a unique nucleotide substitution (1318 C to T) in exon 11, which predicts a substitution of leucine for phenylalanine at residue 440. This substitution is located in a region surrounding the putative structural NADP-binding domain. The markedly abnormal kinetics of glucose-6-phosphate (G6P) of G6PD Kobe suggest the interaction between both NADP and G6P binding sites. AUTHOR. * Hirono, A., Miwa, S., Fujii, H., Ishida, F., Yamada, K., and Kubota, K. Molecular study of eight Japanese cases of glucose-6-phosphate dehydrogenase deficiency by nonradioisotopic single-strand conformation polymorphism analysis. Blood 83:3363-3368, 1994. * Hirono, A. Personal communication , 1994. Notes: G6PD Urayasu 281-283 del; G6PD Chikugo 535A->T;G6PD Tsukui

561-7 CTCCTCC->CTCC; G6PD Seoul 916G->A; G6PD Fukaya 1462G->A. * Johnson, R.M., Ravindranath, Y., El-Alfy, M., and Goyette, G.,Jr. Oxidant damage to erythrocyte membrane in glucose-6-phosphate dehydrogenase deficiency: Correlation with in vivo reduced glutathione concentration and membrane protein oxidation. Blood 83:1117-1123, 1994. * Kaplan, M., Hammerman, C., Kvit, R., Rudensky, B., and Abramov, A. Neonatal screening for glucose-6-phosphate dehydrogenase deficiency: Sex distribution. Arch.Dis.Child.Fetal Neonatal 71:F59-F60, 1994. Notes: Eight hundred and six newborn infants at high risk for glucose-6-phosphate dehydrogenase (G-6-PD) deficiency were screened; 30.2% of the boys and 10.4% of the girls had severe G-6- PD deficiency. Surprisingly, 14% of the enzyme deficient girls had a father from a low risk ethnic group. Girls of high risk mothers should be screened for G-6-PD deficiency regardless of paternal origin. * Kletzien, R.F., Harris, P.K.W., and Foellmi, L.A. Glucose-6-phosphate dehydrogenase: A "housekeeping" enzyme subject to tissue-specific regulation by hormones, nutrients, and oxidant stress. FASEB J. 8:174-181, 1994. Notes: The enzyme, glucose-6-phosphate dehydrogenase (G6PDH, EC1.1.1.49), has long been considered and studied as the archetypical X-linked "housekeeping" enzyme that is present in all cells. where it plays the key role in regulating carbon flow through the pentose phosphate pathway. Specifically, the enzyme catalyzes the first reaction in the pathway leading to the production of pentose phosphates and reducing power in the form of NADPH for reductive biosynthesis and maintenance of the redox state of the cell. It was in this latter function that the crucial importance of the enzyme was first appreciated with the description of the human deficient syndrome. While the gene can be considered to be a constitutively expressed "housekeeping" gene in many tissues, there are several other tissues (liver, adipose, lung, and proliferating cells) wherein modulation of cellular G6PDH activity represents an important component of the integrated response to external stimuli (hormones, growth factors, nutrients, and oxi * Kumar, P., Sarkar, S., and Narang, A. Acute intravascular haemolysis following exchange transfusion with G-6-PD deficient blood. Eur.J.Pediatr. 153:98-99, 1994. Notes: A neonate with hyperbilirubinaemia who developed massive intravascular haemolysis following exchange transfusion with glucose-6-phosphate dehydrogenase deficient blood is described. It is recommended that in areas endemic for this enzyme deficiency the donor blood should be screened before being used for exchange transfusion. AUTHOR. * Lo, Y.S., Lu, C.C., Chiou, S.S., Chen, B.H., Chang, T.T., and Chang, J.G. Molecular characterization of glucose-6-phosphate dehydrogenase deficiency in Chinese infants with or without severe neonatal hyperbilirubinaemia. Br.J.Haematol. 86:858-862, 1994. Notes: To characterize mutations in the glucose-6-phosphate dehydrogenase (G6PD) gene in Chinese infants, we studied 213 G6PD-deficient infants without blood exchange transfusion (BET) therapy, and 34 patients who required BET therapy for their severe hyperbilirubinaemia after birth. Nine different point mutations were characterized in all infants. Of these mutations, the G to T substitution at cDNA nucleotide (nt) 1376, which accounts for the mutations in 131 (53.0%) neonates, followed by

G to A substitution at nt 1388 in 18 (10.5%) infants, A to G substitution at nt 493 in 17 (6.9%) infants, A to G substitution at nt 95 in 10 (4.1%) infants, C to T substitution at nt 1024 in six (2.4%) infants, and G to T substitution at nt 392 in three (1.2%) infants, G to A substitution at nt 487 in two (0.8%) infants, C to T substitution at nt 1360 in two (0.8%) infants and C to T substitution at nt 592 in two (0.8%) infants. Mutations in 48 (19.5%) G6PD- deficient infants were not characterized. Most (64.7%) mutation * Martin, S.K. The malaria/G6PD hypothesis revisited. Parasitol.Today 10:251-252, 1994. * Mason, P.J., Vulliamy, T.J., Bautista, J.M., Luzzatto, L., Naylor, C., and Adams, M. The three dimensional structure of G6PD helps to explain G6PD deficiency. Blood 84(Suppl):14a, 1994. * Nafa, K., Reghis, A., Osmani, N., Baghli, L., A t-Abbes, H., Benabadji, M., Kaplan, J.-C., Vulliamy, T., and Luzzatto, L. At least five polymorphic mutants account for the prevalence of glucose-6-phosphate dehydrogenase deficiency in Algeria. Hum.Genet. 94:513-517, 1994. Notes: The electrophoretic mobility and level of enzyme activity of glucose-6-phosphate dehydrogenase (G6PD) was established in 100 unrelated Algerian males with G6PD deficiency. DNA from these subjects was analysed for the presence of certain known G6PD mutations by the appropriate restriction enzyme digestion of fragments amplified by the polymerase chain reaction. Where the mutation could not be identified in this way, the samples were subjected to single-strand conformation polymorphism analysis and abnormal fragments were sequenced. In this way, eight different mutations have been identified, of which five are polymorphic and account for 92% of the samples. The most common variants are G6PD A- (46%) and G6PD Mediterranean (23%), both of which were associated with favism. A new polymorphic variant, G6PD Aures, has been identified during the course of this study, whereas another, G6PD Santamaria, has now been established as a polymorphic variant (11%). Thus, G6PD deficiency in Algeria is heterogeneous, * Nesterova, T.B., Mazurok, N.A., Matveeva, N.M., Shilov, A.G., Yantsen, E.I., Ginsburg, E.K., Goss, S.J., and Zakian, S.M. Demonstration of the X-linkage and order of the genes GLA, G6PD, HPRT, and PGK in two vole species of the genus Microtus. Cytogenet.Cell Genet. 65:250-255, 1994. * O'Brien, E., Kurdi-Haidar, B., Wanachiwanawin, W., Carvajal, J.-L., Vulliamy, T.J., Cappadoro, M., Mason, P.J., and Luzzatto, L. Cloning of the glucose 6-phosphate dehydrogenase gene from Plasmodium falciparum. Mol.Biochem.Parasitol. 64:313-326, 1994. Notes: Glucose 6-phosphate dehydrogenase (G6PD) deficiency is one of the human genetic traits that confer relative resistance against malaria caused by Plasmodium falciparum. It has been previously shown that this organism, during its intraerythrocytic development, produces its own G6PD, which has properties different from those of human G6PD. In order to investigate the role of this enzyme in parasite-host cell interactions, we have isolated the G6PD gene from Plasmodium falciparum as a set of overlapping lambda gt11 clones. By sequence analysis we have found a single open reading frame, uninterrupted by introns, coding for a protein of 910 amino acids, almost twice as long as any previously sequenced G6PD molecule. The P. falciparum G6PD mRNA is 5.1 kb in size and has an exceptionally long 5' untranslated region of some 1000 nucleotides. We have mapped the

G6PD gene to chromosome 14. The C-terminal portion of the predicted protein, from amino acid 310-910 (except for an 'insert' of 62 amino acids), has 3 * Ong, S.J. and Kearney, B. Local swimming pool and G-6-PD deficiency. Med.J.Aust. 161:226-227, 1994. * Philippe, M., Larondelle, Y., Lemaigre, F., Mariame, B., Delhez, H., Mason, P., Luzzatto, L., and Rousseau, G.G. Promoter function of the human glucose-6-phosphate dehydrogenase gene depends on two GC boxes that are cell specifically controlled. Eur..J.Biochem. 226:377-384, 1994. Notes: Human glucose-6-phosphate dehydrogenase is expressed in all cells by a housekeeping gene whose regulatory 5'-flanking sequence includes at least nine GC boxes. By transient transfection of HeLa and HepG2 cells with constructs containing glucose- 6-phosphate dehydrogenase gene regions linked to a reporter gene, we have now delineated the core promoter and have located upstream stimulatory and inhibitory sequences. By mutational analysis, we demonstrate that the activity of the core promoter requires two out of seven GC boxes. We show that stimulatory protein 1 (Sp1)-related factors and activator protein 2 (AP-2)-related proteins bind to these two boxes in band-shift experiments. One point mutation that affects the binding of only the Sp1-related factors to one or both boxes causes a marked decrease of promoter activity in HepG2 cells but not in HeLa cells. We conclude that (a) two out of many seemingly redundant GC boxes are necessary to drive a G+C-rich housekeeping promoter; (b) factors that bind t * Rank, K.B., Harris, P.K., Ginsberg, L.C., and Stapleton, S.R. Isolation and sequence of a rat glucose-6-phosphate dehydrogenase promoter. Biochim.Biophys.Acta 1217:90-92, 1994. Notes: A 935 bp fragment of the rat glucose-6-phosphate dehydrogenase (G6PDH) gene containing promoter activity was isolated using the polymerase chain reaction (PCR). This fragment was sequenced and primer extension analysis showed a transcription initiation site in agreement with the human and mouse genes. Computer analysis of the sequence showed a 60% and 78% similarity to the human and mouse G6PDH sequences, respectively. A TATA box element, TTAAAT, was found and shown to be 100% similar to the human and mouse TATA box elements. Based on sequence comparison, some putative transcriptional regulatory elements were also found. AUTHOR. * Rovira, A., Vulliamy, T.J., Pujades, A., Luzzatto, L., and Vives Corrons, J.-L. The glucose-6-phosphate dehydrogenase (G6PD) deficient variant G6PD Union (454 Arg-->Cys) has a worldwide distribution possibly due to recurrent mutation. Hum.Mol.Genet. 3:833-835, 1994. * Saha, N., Ramzan, M., Tay, J.S.H., Low, P.S., Basair, J.B., and Khan, F.M. Molecular characterisation of red cell glucose-6-phosphate dehydrogenase deficiency in North-West Pakistan. Hum.Hered. 44:85-89, 1994. Notes: 233 Pushtoons (129 males and 104 females), 51 Punjabi Muslims (29 males and 22 females) and 21 Afghans (15 males and 6 females) were screened for the presence of red cell glucose6-phosphate dehydrogenase (G6PD) variants by a dye decolouration screening test and starch gel electrophoresis. The overall frequency of G6PD deficiency in males was found to be about 10%. 17 male G6PD-deficient samples were further investigated for the C -> T substitution at nucleotide (nt) 563 (the Mediterranean mutation) and the C -> T substitution at nt 1311 (the 'silent' allele) of the G6PD gene by PCR amplification followed by

digestion with appropriate restriction enzymes. 10 of the 13 Pushtoon 2 Punjabi and 1 Afghan males had the 563 mutations. Only 1 (Punjabi) out of 13 G6PD- deficient males with the 563 mutation had the silent mutation at nt 1311. The frequency of the silent mutation was found to be about 0.20 in the 60 Pushtoon and 19 Punjabi non-deficient males. AUTHOR. * Saha, S., Saha, N., Tay, J.S.H., Jeyaseelan, K., Basair, J.B., and Chew, S.E. Molecular characterisation of red cell glucose-6-phosphate dehydrogenase deficiency in Singapore Chinese. Am.J.Hematol. 47:273-277, 1994. Notes: Sixty-two G6PD deficient Chinese males have been investigated for the presence of seven mutations of the coding region of the G6PD gene by natural and artifically created amplified restriction sites. The results show that the G to T substitution at nucleotide (nt) 1376 and G to A substitution at nt 1388 represent 24% and 21% of G6PD deficiency, respectively, in the Singapore Chinese; 37% of the sample could not be characterised. The remaining samples were identified as follows: 10% C --> T at nt 563, 5% A --> G at nt 95, and 3% C --> T at nt 1024. The G to A substitution (nt 487) and the substitution A --> G (nt 493) were not present in this sample. None of the subjects with the Mediterranean mutation (563 C --> T) had the silent mutation at 1311 (C --> T). This study confirms the extreme molecular heterogeneity of the G6PD gene in the Chinese. (C) 1994 Wiley-Liss, Inc. * Shahabuddin, M., Rawlings, D.J., and Kaslow, D.C. A novel glucose-6-phosphate dehydrogenase in Plasmodium falciparum: cDNA and primary protein structure. Biochim.Biophys.Acta 1219:191-194, 1994. Notes: The structure of the parasite-encoded G6PD (PfG6PD) may provide clues about the relative protection against malaria in humans with glucose-6-phosphate dehydrogenase (G6PD) deficiency. We have cloned Pfg6pd cDNA encoding a predicted 856 amino acid residues polypeptide with a calculated molecular mass of > 94 kDa. The predicted amino acid sequence is highly homologous to G6PD from other organisms. Pfg6pd maps as a single or low copy number gene to chromosome 14. The unusually large N-terminus and the distance between the NADP-binding site and G6PD-binding site is novel for the parasite G6PD. The differences between parasite and human G6PD proteins could potentially be exploited for designing new chemotherapeutic agents. * Stockham, S.L., Harvey, J.W., and Kinden, D.A. Equine glucose-6-phosphate dehydrogenase deficiency. Vet.Pathol. 31:518-527, 1994. Notes: Glucose-6-phosphate dehydrogenase (G6PD) deficiency is a well-characterized X-linked inherited disorder in humans but has not been reported in horses. We describe a persistent hemolytic anemia and hyperbilirubinemia due to a severe G6PD deficiency in an American Saddlebred colt. Other abnormalities in the colt's erythrocytes as compared with those of healthy horses (n = 22-35) included increased activities of hexokinase and pyruvate kinase, decreased concentrations of reduced glutathione and reduced nicotinamide adenine dinucleotide phosphate (NADP), and increased concentration of oxidized NADP. Morphologic abnormalities included eccentrocytosis, pyknocytosis, anisocytosis, macrocytosis, and increased number of Howell-Jolly bodies. Scanning and transmission electron microscopic examinations revealed that eccentrocytes had contracted to spherical regions and thin collapsed regions. Eccentrocytes were more electron dense than were normal erythrocytes when examined by transmission

electron microscopy.. * Swart, M.K.J., Bissbort, S., Ferguson, J.W.H., and Ungerer, J.P.J. Polymorphism of glucose-6-phosphate dehydrogenase in black rhinoceroses: A possible link with haemolytic anaemia. S.Afr.J.Sci. 90:14-16, 1994. Notes: The high incidence of haemolytic anaemia in black rhinoceroses (Diceros bicornis) is a matter of concern to conservationists because of the mortality attributed to this syndrome during capture or handling operations: intravascular haemolytic episodes may be induced in animals by oxidative stress and often those episodes are fatal. Blood samples of 105 black rhinoceroses from different natural habitats were investigated and a genetic polymorphism of the erythrocyte enzyme glucose6-phosphate dehydrogenase (G-6PD) is described. This is the first time a polymorphism for this enzyme has been described for a wild animal: a deficiency of the enzyme in humans is associated with intravascular haemolysis. Two common alleles resulting in three phenotypes were detected by means of starch gel electrophoresis and specific enzyme staining. The gene product of the variant allele, an anodally faster migrating enzyme, showed a markedly reduced activity ((approx.) 50%) compared to the 'normal', slow isoenzyme. The a * Tang, T.K., Yeh, C.-H., Huang, C.-S., and Huang, M.-J. Expression and biochemical characterization of human glucose6-phosphate dehydrogenase in Escherichia coli: A system to analyze normal and mutant enzymes. Blood 83:1436-1441, 1994. * Toren, A., Brok-Simoni, F., Ben-Bassat, I., Holtzman, F., Mandel, M., Neumann, Y., Ramot, B., Rechavi, G., and Kende, G. Congenital haemolytic anaemia associated with adenylate kinase deficiency. Br.J.Haematol. 87:376-380, 1994. Notes: Chronic haemolytic anaemia associated with adenylate kinase (AK) deficiency is very rare and only seven cases in five families have been described. We present six children of one family who are deficient of this enzyme and in three of them a combined G6PD deficiency was found. AK deficiency was transmitted by an autosomal recessive gene and heterozygous state was not accompanied by disease, whereas homozygously affected individuals present a congenital chronic non-spherocytic haemolytic anaemia with haemoglobin levels of 8-9 g/dl. Patients also deficient in G6PD suffer from a more severe haemolytic anaemia with haemoglobin levels around 6 g/dl. The AK-deficient children are also mentally retarded. Splenectomy performed in five of the six patients resulted in complete remission of the haemolytic process. * Valaes, T. Severe neonatal jaundice associated with glucose-6-phosphate dehydrogenase deficiency: Pathogenesis and global epidemiology. Acta Paediatr. 83 Suppl. 394:58-76, 1994. Notes: The association of glucose-6-phosphate dehydrogenase deficiency (G6PD def) with severe neonatal jaundice (NJ) and Kernicterus was described just over 30 years ago in reports from Sardinia (1-4) Singapore (5,6) and Greece (7,8). In this review we will examine the progress made since that time in our understanding of the pathophysiology of severe NJ associated with G6PD def, its global epidemiology, and its role in the balanced polymorphism of the G6PD def gene (Gd). Including this review in the Festschrift to Spyros Doxiadis should highlight his contribution to the field. In Greece the search for a new cause of severe NJ and Kernicterus was triggered by his realization that the recognized at the time, causes of severe NJ were absent in a large proportion of the neonates treated at the "Alexandra"

Maternity Hospital in Athens (9). * Vives Corrons, J.L., Rovira, A., Pujades, M.A., Estrada, M., and Vulliamy, T.J. Diverse point mutations of glucose-6-phosphate dehydrogenase (G6PD) gene in Spanish and Cuban patients with hemolytic anaemia. La Revista de Investigacion Clinica 46(Suppl):234a, 1994. Notes: Clinic 1251G; Union 1360T; 1155G; 209G; 406C; "Santamaria" 542T. * Al-Ali, A.K., Ahmed, M.A.M., Qaw, F.S., Al-Fadel Saleh, M., and Al-Bashir, A. Uric acid, creatinine and urea in normal, glucose-6-phosphate dehydrogenase-deficient and Hb SS Saudi subjects. Acta Haematol.(Basel) 94(2):114-116, 1995. * Ardati, K.O., Bajakian, K.M., Mohammad, A.M., and Coe, E.L. Glucose-6-phosphate dehydrogenase phenotypes in Bahrain: Quantitative analysis and electrophoretic characterization. Saudi Med.J. 16:102-104, 1995. * Bautista, J.M., Mason, P.J., and Luzzatto, L. Human glucose-6-phosphate dehydrogenase lysine 205 is dispensable for substrate binding but essential for catalysis. FEBS Lett. 366(1):61-64, 1995. Notes: By site-directed mutagenesis of the cloned human glucose-6- phosphate dehydrogenase cDNA, lysine 205 (the residue that after reacting with pyridoxal-5'-phosphate renders inactive enzyme) was mutated to threonine (K205T) to remove the amino group, or to arginine (K205R) to displace the position of the amino group, in order to analyze the role of its nucleophilic group in position epsilon. Compared to the wild-type enzyme, the K205T and K205R mutants retain a specific activity of 2.6 and 11.4%, respectively; their catalytic specificity (K-cat/K-m) is drastically decreased, whereas the K-m values for both substrates are only slightly increased, These findings in the light of the 3D structure of G6PD suggest that the epsilon-amino group of lysine 205 can favour a hydrogen bond within the active pocket essential for catalysis. * Beutler, E. Deficit en G6PD: Pathologie moleculaire. Hematologie 1:385-392, 1995. Notes: (MS434) (B1024). * Beutler, E., Westwood, B., Melemed, A., Dal Borgo, P., and Margolis, D. Three new exon 10 glucose-6-phosphate dehydrogenase mutations. Blood Cells Mol.Dis. 21:64-72, 1995. Notes: (MS449) (B1009) Three previously undescribed mutations of the glucose-6- phosphate dehydrogenase (G6PD) gene have been documented in pahereditary non-spherocytic hemolytic anemia (HNSHA). In none of the cases have we been able to obtain a sufficient volume of blood to characterize the residual enzyme biochemically. "G6PD Calvo Mackenna" was due to an A G transition in cDNA nucleotide 1138 creating an Aat II site and resulting in a substitution of valine for isoleucine at amino acid 380. "G6PD Riley" was due to a T C transition at cDNA nucleotide 1139 also changing the 380 isoleucine, in this case to a threonine. "G6PD Wisconsin" was due to an C G transversion in cDNA nucleotide 1177, destroying a Aci I site and resulting in a substitution of glycine for arginine at amino acid 393. All of these mutations were in exon 10, where mutations that cause HNSHA appear to be clustered. We present a list of the 83 mutations of G6PD that have been documented to the end of April, 1995. AUTHOR. * Beutler, E. Glucose-6-phosphate dehydrogenase deficiency and other enzyme abnormalities. In: Hematology, edited by Beutler, E., Lichtman, M.A., Coller, B.S., and Kipps, T.J.New York:McGraw-Hill, 1995,p. 564-580.

Notes: B1027. * Camardella, L., Damonte, G., Carratore, V., Benatti, U., Tonetti, M., and Moneti, G. Glucose 6-phosphate dehydrogenase from human erythrocytes: Identification of N-acetyl-alanine at the N-terminus of the mature protein. Biochem.Biophys.Res.Commun. 207:331-338, 1995. Notes: Glucose 6-phosphate dehydrogenase from human erythrocytes has a blocked amino-terminus and no information could be obtained by direct sequencing of the intact protein. The peptide corresponding to the amino-terminal region was isolated from a tryptic digest of the whole protein and identified on the basis of its amino acid composition and of the failure to obtain Edman degradation. Determination of peptide mass by fast atom bombardment mass spectrometry allowed identification of the blocked amino-terminal residue as N-acetyl-alanine. (C) 1995 Academic Press,Inc. * Cappellini, M.D., Martinez di Montemuros, F., Dotti, C., Tavazzi, D., and Fiorelli, G. Molecular characterisation of the glucose-6-phosphate dehydrogenase (G6PD) Ferrara II variant. Hum.Genet. 95:440-442, 1995. Notes: During the last ten years, molecular biological techniques such as cloning and sequencing and, more recently, polymerase chain reaction (PCR) amplification have led to the identification of the molecular defects responsible for more than fifty glucose-6-phosphate dehydrogenase (G6PD) variants. In this paper, we report the identification of the molecular abnormality underlying the G6PD Ferrara II variant, present in the Po delta area of Northern Italy. Biochemical characterisation shows an enzymatic activity of about 15% of normal (WHO class III), slow electrophoretic mobility, low Km for G6P, high percentage substrate analogue utilisation and a biphasic pH optimum curve. After PCR amplification, non-radioisotopic single-strand conformation polymorphism analysis carried out for the entire coding region has revealed a mobility shift in exon 8. Nucleotide sequencing has demonstrated a missense 844 G>C mutation, causing an Asp>His amino-acid replacement, known as being responsible for G6PD Seattle, G6PD * Chang, J.-G. and Liu, T.-C. Glucose-6-phosphate dehydrogenase deficiency. Crit.Rev.Oncol.Hematol. 20(1-2):1-7, 1995. * Efferth, T., Fabry, U., Glatte, P., and Osieka, R. Increased induction of apoptosis in mononuclear cells of a glucose-6-phosphate dehydrogenase deficient patient. Clin.Investig. 73:47-49, 1995. Notes: Glucose-6-phosphate dehydrogenase (G6PD) deficiency belongs to the most common human disorders of metabolism. In affected patients generation of free radicals causes life-threatening hemolytic crises, for example, after consumption of certain drugs and foods or after infections. Rather than erythrocytes we analyzed mononuclear white blood cells of a patient suffering from G6PD deficiency with respect to their ability to enter apoptosis after treatment with daunorubicin, ionizing radiation, or dexamethasone. The induction of apoptosis was increased in G6PD-deficient cells compared to cells from eight normal donors. In parallel, the glutathione content of mononuclear cells from the G6PD-deficient patient was significantly decreased. While in affected patients decreased life span of erythrocytes damaged by oxidative stress has long been recognized as the mechanism underlying hemolysis, peripheral leukocytes have not received similar attention. Induction of

apoptosis is a relatively complex process that * El-Hazmi, M.A.F., Al-Swailem, A., and Warsy, A.S. Glucose-6-phosphate dehydrogenase deficiency and sickle cell genes in Bisha. J.Trop.Pediatr. 41(4):225-229, 1995. Notes: This study was conducted on 820 Saudi males and females from Bisha in the western province of Saudi Arabia. Blood samples were analysed to determine the frequency of glucose-S-phosphate dehydrogenase deficiency and haemoglobin S (Hb S) genes, and to investigate interactions between the two genes. Severe G-6-PD deficiency in this population was due to G-6-PD-Mediterranean; the African variant G-6-PD-A(-) was not detected. The normal and common form of the enzyme was G-6-PD-B+, occurring at a frequency of 0.8444 and 0.8177 in males and females, respectively. Variants included G-6-PD-A(+), G-6-PD-Mediterranean, and G-6-PD-Mediterranean-like at frequencies of 0.0043, 0.0767, and 0.0746, respectively, in males and 0.0057, 0.05413, and 0.0855, respectively, in females. Sickle cell haemoglobin (Hb S) was encountered in the homozygous (4 per cent) and heterozygous (10 per cent) states at a gene frequency of 0.0860. No interaction between G-6-PD deficiency and Hb S gene was observed. A severe haematological * Ganczakowski, M., Town, M., Bowden, D.K., Vulliamy, T.J., Kaneko, A., Clegg, J.B., Weatherall, D.J., and Luzzatto, L. Multiple glucose 6-phosphate dehydrogenase-deficient variants correlate with malaria endemicity in the Vanuatu archipelago (southwestern Pacific). Am.J.Hum.Genet. 56:294-301, 1995. Notes: In studying the relationship between genetic abnormalities of red blood cells and malaria endemicity in the Vanuatu archipelago in the southwestern Pacific, we have found that of 1,442 males tested, 98 (6.8%) were G6PD deficient. The prevalence of GdPD deficiency varied widely (0%-39%), both from one island to another and in different parts of the same island, and generally correlated positively with the degree of malaria transmission. The properties of G6PD from GdPD-deficient subjects were analyzed in a subset of 53 samples. In all cases the residual red-blood-cell activity was <10%. There were three phenotypic patterns. PCR amplification and sequencing of the entire coding region of the G6PD gene showed that the first of these patterns corresponded to G6PD Union (nucleotide 1360C-->T; amino acid 454Arg-->Cys), previously encountered elsewhere. Analysis of samples exhibiting the second pattern revealed two new mutants: G6PD Vanua Lava (nucleotide 383T-->C; amino acid 128Leu--> Pro) and G6PD Namoru * Ganea, E. and Harding, J.J. Molecular chaperones protect against glycation-induced inactivation of glucose-6-phosphate dehydrogenase. Eur.J.Biochem. 231(1):181-185, 1995. Notes: Glucose-6-phosphate dehydrogenase is inactivated slowly by reaction with sugars (glycation), a process thought to be important in the development of diabetic complications. A major protein from the ocular lens, alpha-crystallin. which exhibits some chaperone-like properties, protects against this inactivation. The well-known molecular chaperone GroEL (chaperonin 60 from Escherichia coli) also protects. On a molar basis, alpha-crystallin is better than GroEL at protecting against glycation-induced inactivation of glucose-6-phosphate dehydrogenase. The relative amounts of enzyme/chaperone indicate that each molecule of alpha-crystallin binds two molecules of the damaged enzyme. This supports the view that alpha-crystallin has a chaperone-like structure as well as a chaperone-like function. * Gangarossa, S., Romano, V., Del Giudice, E.M., Perrotta,

S., Iolascon, A., and Schiliro, G. Congenital dyserythropoietic anemia type II associated with G6PD Seattle in a Sicilian child. Acta Haematol.(Basel) 93(1):36-39, 1995. Notes: A 2-year-old Sicilian boy was investigated because of chronic nonspherocytic hemolytic anemia (CNSHA) associated with hepatosplenomegaly. Appropriate studies revealed deficiency of glucose-6-phosphate dehydrogenase type Seattle (G6PD Seattle). In addition, bone marrow morphology, serological studies and analysis of red cell membrane proteins revealed congenital dyserythropoietic anemia (CDA) type II (or HEMPAS). Because G6PD Seattle on its own does not cause CNSHA, we believe that the clinical manifestations in this patient are essentially due to the CDA type II abnormality. However, the coexistence of these two different red cell abnormalities may affect the clinical picture specifically by making CDA type II more hemolytic than it would have been otherwise. * Grossman, S., Budinsky, R., and Jollow, D. Dapsone-induced hemolytic anemia: Role of glucose-6-phosphate dehydrogenase in the hemolytic response of rat erythrocytes to N-hydroxydapsone. J.Pharmacol.Exp.Ther. 273(2):870-877, 1995. Notes: Individuals deficient in erythrocytic glucose-6-phosphate dehydrogenase (G6PD) show about a 2-fold increase in sensitivity toward dapsone-induced hemolytic anemia. Rat studies have shown that the hemolytic activity of dapsone resides in its N-hydroxy metabolites; exposure of rat red cells to N-hydroxydapsone in vitro followed by readministration to isologous rats results in premature splenic sequestration of the damaged cells. This study examines the ability of the steroid, epiandrosterone, to inhibit rat red cell G6PD and the effect of such inhibition on the susceptibility of rat red cells to N-hydroxydapsone hemolytic activity. Epiandrosterone was found to inhibit rat red cell G6PD uncompetitively and to suppress red cell hexose monophosphate shunt activity by more than 95%. Epiandrosterone suppression of rat red cell G6PD activity resulted in about a 2-fold increase in sensitivity of the rat cells to N-hydroxydapsone hemolytic activity, and a modest but significant increase in depletion of red ce * Hirono, A., Fujii, H., and Miwa, S. Identification of two novel deletion mutations in glucose- 6-phosphate dehydrogenase gene causing hemolytic anemia. Blood 85:1118-1121, 1995. Notes: Among over 50 distinct mutations causing glucose-6-phosphate dehydrogenase (G6PD) deficiency, only two deletion mutations have so far been reported. Using nonradioisotopic single- strand conformation polymorphism analysis, we found two additional deletion mutations in two Japanese G6PD-deficient patients with nonspherocytic hemolytic anemia, Case no. 1 had a 3-nucleotide deletion in exon 6 predicting a deletion of a serine at amino acid 188 or 189, which caused a class 1 variant GGPD Tsukui, Case no, 2 had a 3-nucleotide deletion in exon 5 predicting a deletion of a lysine at residue 95, which caused a class 2 variant G6PD Urayasu. The 188th serine, which might be deleted in G6PD Tsukui, is located close to the putative G6P binding site, The 188th serine is also involved in the amino acid substitution in G6PD Mediterranean, but the kinetics of these two variants are totally different. The residue with an amino acid deletion in G6PD Urayasu was distant from the substrate binding sites and was located * Hirono, A., Ishii, A., Kere, N., Fujii, H., Hirono, K., and Miwa, S. Molecular analysis of glucose-6-phosphate dehydrogenase variants in the Solomon Islands. Am.J.Hum.Genet. 56:1243-1245,

1995. * Horn, S., Bashan, N., Peleg, N., and Gopas, J. Membrane glycoprotein modifications of G6PD deficient red blood cells. Eur.J.Clin.Invest. 25:32-38, 1995. Notes: In this study, the composition and the role of membrane glycoproteins in phagocytosis were determined in G6PD deficient RBCs. G6PD deficient RBCs were recognized and significantly phagocytosed by murine macrophages, without pre-exposure to oxidants in vivo. Phagocytosis was partially (60%) inhibited by incubating macrophages with either galactose or mannose, or by incubating RBCs with beta-galactosidase, indicating the involvement of lectin-like receptors in the recognition of G6PD deficient RBCs. Membrane glycoproteins on G6PD deficient cells were detected by binding of Con A to both intact RBCs and to purified membrane proteins. The results demonstrated modifications in the glycoprotein pattern of G6PD deficient RBCs compared to untreated controls. These included reduction in the amounts of several high molecular weight glycoproteins and appearance of lower molecular weight bands. These results suggest that G6PD deficient RBCs undergo glycoprotein modifications, which may lead to premature removal * Kaeda, J.S., Chhotray, G.P., Ranjit, M.R., Bautista, J.M., Reddy, P.H., Stevens, D., Naidu, J.M., Britt, R.P., Vulliamy, T.J., Luzzatto, L., and Mason, P.J. A new glucose-6-phosphate dehydrogenase variant, G6PD Orissa (44 Ala-->Gly), is the major polymorphic variant in tribal populations in India. Am.J.Hum.Genet. 57(6):1335-1341, 1995. Notes: Deficiency of glucose-6-phosphate dehydrogenase (G6PD) is usually found at high frequencies in areas of the world where malaria has been endemic. The frequency and genetic basis of G6PD deficiency have been studied in Africa, around the Mediterranean, and in the Far East, but little such information is available about the situation in India. To determine the extent of heterogeneity of G6PD, we have studied several different Indian populations by screening for G6PD deficiency, followed by molecular analysis of deficient alleles. The frequency of G6PD deficiency varies between 3% and 15% in different tribal and urban groups. Remarkably, a previously unreported deficient variant, G6PD Orissa (44 Ala-->Gly), is responsible for most of the G6PD deficiency in tribal Indian populations but is not found in urban populations, where most of the G6PD deficiency is due to the G6PD Mediterranean (188 Ser-->Phe) variant. The K-m(NADP) of G6PD Orissa is fivefold higher than that of the normal enzyme. This may be d * Kaplan, M. and Hammerman, C. Glucose-6-phosphate dehydrogenase deficiency. Postgrad.Med.J. 71(842):765, 1995. * Luzzatto, L. About hemoglobins, G6PD and parasites in red cells. Experientia 51:206-208, 1995. * Luzzatto, L., Mehta, A., and Meloni, T. Haemoglobinuria and haptoglobin in G6PD deficiency. Br.J.Haematol. 91(2):511-512, 1995. * MacDonald, M.G. Hidden risks: Early discharge and bilirubin toxicity due to glucose 6-phosphate dehydrogenase deficiency. Pediatrics 96(4 PT 1):734-738, 1995. * Mason, P.J., Sonati, M.F., MacDonald, D., Lanza, C., Busutil, D., Town, M., Corcoran, C.M., Kaeda, J.S., Stevens, D.J., Al-Ismail, S., Altay, C., Hatton, C., Lewis, D.S., McMullin, M.F., Meloni, T., Paul, B., Pippard, M., Prentice, A.G., Vulliamy, T..J., and Luzzatto, L. New glucose-6-phosphate dehydrogenase mutations associated with chronic anemia. Blood

85:1377-1380, 1995. Notes: We have identified the glucose-6-phosphate dehydrogenase mutations responsible for enzyme deficiency in nine individuals with chronic nonspherocytic hemolytic anemia. We found the variants Tokyo, Iowa, Shinshu, and Guadalajara in British subjects and Kobe in an Italian. In addition we have determined the variant Corum has the mutation 820 G --> A and have found in British subjects the mis-sense mutations 224 T --> C, 488 G --> A and 833 C --> T which have not been described before. Some, but not all, of the mutations involve amino acids located near putative substrate binding sites. (C) 1995 by The American Society of Hematology. * Mason, P.J., Stevens, D.J., Luzzatto, L., Brenner, S., and Aparicio, S. Genomic structure and sequence of the Fugu rubripes glucose- 6-phosphate dehydrogenase gene (G6PD). Genomics 26:587-591, 1995. Notes: To investigate the organization of the compact genome of the puffer fish Fugu rubripes at the level of an individual housekeeping gene, we have cloned and sequenced the glucose6-phosphate dehydrogenase (G6PD) gene from this fish and compared it to the corresponding human gene. The intron/exon structure of the two genes is identical throughout the protein coding regions, The puffer fish gene is four times smaller than the human gene-the difference is accounted for by the fact that the puffer fish gene has smaller introns. Intron 2 is the largest intron in both species. We have constructed a molecular phylogeny for 10 G6PD protein sequences. The sequences fall in the expected arrangement based on established phylogenetic relationships, with the Plasmodium falciparum sequence the most widely diverged. (C) 1995 Academic Press, Inc. * Medina, M.D., Vaca, G., Esparza, A., Westwood, B., and Beutler, E. Molecular heterogeneity of G-6-PD deficiency in Mexico. Arch.Med.Res. 26(2):111-113, 1995. Notes: (B1048) (MS416) DNA samples from seven G-6-PD deficient Mexican mestizo patients were analyzed. Three different G-6-PD genotypes were observed: G- 6-PD A-202A/376G (three patients), G-6-PD A-376G/968C (three patients) and G-6-PD Seattle844C. The present results, along with previous reports, suggest not only G-6-PD A-genotypes are relatively common but also G-6-PD deficiency seems to be heterogeneous at DNA level in Mexico. * Oo, M., Tin-Shwe, Marlar-Than, and O'Sullivan, W.J. Genetic red cell disorders and severity of falciparum malaria in Myanmar. Bull.World Health Organ. 73(5):659-665, 1995. Notes: A hospital-based survey was undertaken to investigate the relationship between the incidence and severity of malaria infection and various red cell disorders in Myanmar. The mean parasitaemia levels of patients with alpha- or beta-thalassaemia trait or with severe glucose-6-phosphate dehydrogenase (G6PD) deficiency were lower than those of individuals with normal haemoglobin AA or with heterozygous haemoglobin E. The double genetic defect of thalassaemia trait and severe G6PD deficiency appeared to confer some degree of protection against malaria. * Pandolfi, P.P., Sonati, F., Rivi, R., Mason, P., Grosveld, F., and Luzzatto, L. Targeted disruption of the housekeeping gene encoding glucose 6-phosphate dehydrogenase (G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress. EMBO J. 14(21):5209-5215, 1995. Notes: Glucose 6-phosphate dehydrogenase (G6PD) is a housekeeping enzyme encoded in mammals by an X-linked gene. It has important functions in intermediary metabolism because it catalyzes the

first step in the pentose phosphate pathway and provides reductive potential in the form of NADPH. In human populations, many mutant G6PD alleles (some present at polymorphic frequencies) cause a partial loss of G6PD activity and a variety of hemolytic anemias, which vary from mild to severe. All these mutants have some residual enzyme activity, and no large deletions in the G6PD gene have ever been found. To test which, if any, function of G6PD is essential, we have disrupted the G6PD gene in male mouse embryonic stem cells by targeted homologous recombination. We have isolated numerous clones, shown to be recombinant by Southern blot analysis, in which G6PD activity is undetectable. We have extensively characterized individual clones and found that they are extremely sensitive to H2O2 and to the sulfydryl group oxid * Rodriguez-Cuartero, A., Perez-Blanco, F.J., Sierra, R., Nunez, J., and Mora-Guijosa, A. Erythrocyte glucose 6 phosphate dehydrogenase deficiency in East Andalusia (Spain). Eur.J.Haematol. 54(4):274-275, 1995. * Rovira, A., Vulliamy, T., Pujades, M.A., Luzzatto, L., and Corrons, J.L.V. Molecular genetics of glucose-6-phosphate dehydrogenase (G6PD) deficiency in Spain: Identification of two new point mutations in the G6PD gene. Br.J.Haematol. 91(1):66-71, 1995. Notes: In order to explore the nature of glucose-6-phosphate dehydrogenase (G6PD) deficiency in Spain, we have analysed the G6PD gene in 11 unrelated Spanish G6PD-deficient males and their relatives by using the polymerase chain reaction and single-strand conformation polymorphism (PCR-SSCP) analysis combined with a direct PCR-sequencing procedure and PCR-restriction enzyme (RE) analysis. We have identified eight different missense mutations, six of which have been reported in previously described G6PD variants. In nine patients who had presented with acute favism we found the following mutations: G6PD A-(376G-202A) (four cases), G6PD Union(1360T) (two cases), G6PD Mediterranean(563T) (one case) and G6PD Aures(143C) (one case). In the remaining patient a novel A to G transition was found at nucleotide position 209 which has not been reported in any other ethnic group. This mutation results in a (70) Tyr to Cys substitution and the resulting G6PD variant was biochemically characterized and designated as G6P * Ruwende, C., Khoo, S.C., Snow, R.W., Yates, S.N.R., Kwiatkowski, D., Gupta, S., Warn, P., Allsopp, C.E.M., Gilbert, S.C., Peschu, N., Newbold, C.I., Greenwood, B.M., Marsh, K., and Hill, A.V.S. Natural selection of hemi- and heterozygotes for G6PD deficiency in Africa by resistance to severe malaria. Nature 376(6537):246-249, 1995. Notes: GLUCOSE-6-PHOSPHATE dehydrogenase (G6PD) deficiency, the most common enzymopathy of humans, affects over 400 million people(1). The geographical correlation of its distribution with the historical endemicity of malaria suggests that this disorder has risen in frequency through natural selection by malaria(2.3). However, attempts to confirm that G6PD deficiency is protective in case-control studies of malaria have yielded conflicting results(4-8). Hence, for this X-linked disorder, it is unclear whether both male hemizygotes and female heterozygotes are protected or, as frequently suggested, only females(1,5-11). Furthermore, how much protection may be afforded is unknown. Here we report that, in two large case-control studies of over 2,000 African children, the common African form of G6PD deficiency (G6PD A-) is associated with a 46-58% reduction in risk of severe

malaria for both female heterozygotes and male hemizygotes. A mathematical model incorporating the measured selective advantage against m * Saad, S.T.O., Costa, F.F., Salles, T.S.I., Sonatti, M.F., and Figueiredo, M.S. Glucose-6-phosphate dehydrogenase deficiency in sickle cell disease by DNA analysis. Blood 85:601-602, 1995. * Saha, N., Hong, S.H., Low, P.S., and Tay, J.S.H. Biochemical characteristics of four common molecular variants in glucose-6-phosphate dehydrogenase-deficient Chinese in Singapore. Hum.Hered. 45(5):253-257, 1995. Notes: Biochemical characteristics were determined for four common molecular variants of glucose-6-phosphate dehydrogenase (G6PD) deficiency and 10 non-deficient Chinese males in Singapore. The variants included one Mediterranean (nt563 C --> T), two Canton (G --> T at nt1376) and one each of Kaiping (1388 G --> A) and Chinese-5 (1024 C --> T) variants. Molecular identification was carried out by amplication of genomic DNA with specific oligonucleotide primers followed by digestion with restriction enzymes that recognize artificially created or naturally occurring restriction sites. All the variants had low enzyme activity in red cells (0.2-0.6 IU/g Hb). All but the Chinese-5 variant (nt1024) had a normal K-m for NADP (7-10 mu M). The Mediterranean variant had a high utilization of deamino-NADP (296%), followed by the Canton variant 1376 substitution (131%). The K-m for glucose-6-phosphate was low in the Mediterranean and 1376 variant (18-40 mu M) but high in the 1024 substitution (104 mu M). Electrophoret * Seidman, D.S., Shiloh, M., Stevenson, D.K., Vreman, H.J., Paz, I., and Gale, R. Role of hemolysis in neonatal jaundice associated with glucose-6-phosphate dehydrogenase deficiency. J.Pediatr. 127(5):804-806, 1995. Notes: End-tidal carbon monoxide was measured in 108 newborn infants who had been screened for glucosed-phosphate dehydrogenase (G6PD) deficiency. The mean +/- SD end-tidal carbon monoxide did not differ significantly between the G6PD-deficient and the normal neonates, 2.1 +/- 0.6 mu l/L and 2.0 +/- 0.5 mu l/L, respectively, within 12 hours of birth and 1.9 +/- 1.4 mu l/L and 1.5 +/- 0.7 mu l/L, respectively, at 48 to 72 hours after birth. On the basis of these measurements, hemolysis is not a sufficient explanation for jaundice in G6PD-deficient newborn infants in the transitional period. * Slusher, T.M., Vreman, H.J., McLaren, D.W., Lewison, L.J., Brown, A.K., and Stevenson, D.K. Glucose-6-phosphate dehydrogenase deficiency and carboxyhemoglobin concentrations associated with bilirubin-related morbidity and death in Nigerian infants. J.Pediatr. 126:102-108, 1995. Notes: Our objective was to determine whether glucose-6-phosphate dehydrogenase (G6PD) deficiency and elevated carboxyhemoglobin (COHb) levels correlated with bilirubin-related morbidity and mortality rates. For this purpose, we studied 55 clinically jaundiced infants admitted to a rural mission hospital in southern Nigeria. Total serum bilirubin levels (range, 80 to 1016 mu mol/L (4.7 to 59.4 mg/dl)) correlated with the percentage COHb concentrations (COHb = 0.45 + 0.08(.) Total serum bilirubin; r = 0.72), Infants were divided into two groups of equal size around the median COHb concentration (COHb range, 0.43% to 5.93% (median = 1.40%), with ambient carbon monoxide of 0.65 +/- 0.03 mu L/L). The COHb levels greater than or equal to 1.40% were associated with the need for exchange transfusion (15/28, or 54%, vs 5/27, or 19%; p <0.01) and with an increased incidence of

clinical findings compatible with kernicterus (9/28, or 32%, vs 0/27, or 0%; p <0.01), Mortality rate was 29% (8/29) among infants with high * Soemantri, A.G., Saha, S., Saha, N., and Tay, J.S.H. Molecular variants of red cell glucose-6-phosphate dehydrogenase deficiency in central Java, Indonesia. Hum.Hered. 45(6):346-350, 1995. Notes: One hundred and sixty-nine Javanese males were screened for the presence of red cell glucosed-phosphate dehydrogenase (G6PD) variants by a dye decoloration screening test and starch gel electrophoresis. The frequency of G6PD deficiency was 14%. Three non-deficient electrophoretic variants with mobilities of 95, 105 and 107% of Gd-B+ were encountered. Sixteen G6PD-deficient subjects were further investigated for the presence of mutations at nt95 A-->G, nt487 G-->A, nt493 A->G, nt563 C->T, nt1024 C-->T, nt1376 G-->T, nt1388 G-->A and the silent mutation (nt1311 C-->T) of the G6PD gene by natural or artificially created amplified restriction sites. They were identified by the polymerase chain reaction and electrophoresis of restriction-digested products. Five subjects had the Mediterranean mutation (nt563 C-->T), but only one had simultaneous presence of nt1311(T). The next common mutations were 1376(T) in three subjects and 487(A) in two subjects. Five of the sixteen subjects had the nt1311(T) mutatio * Tan, W. and Yeung, E.S. Simultaneous determination of enzyme activity and enzyme quantity in single human erythrocytes. Anal.Biochem. 226:74-79, 1995. Notes: An integrated laser-based fluorescence enzyme assay and particle-counting immunoassay system with zeptomole sensitivity has been developed for simultaneous determinations of activity and concentration of enzymes in single erythrocytes. The product NADPH of the reaction between glucose-6-phosphate and NADP(+) catalyzed by glucose-6-phosphate dehydrogenase (G6PDH) is monitored. Simultaneously, the agglutination of antibody-coated particles in the presence of G6PDH produces large particles which are counted by light scattering. The correlation between the two parameters indicates that on average only about 35% of the enzyme in individual cells is active. There is more than a 10-fold cell-to-cell variation in the ratios of the two parameters. This indicates that there are multiple mechanisms for the degradation of intracellular enzymes as a function of cell age. (C) 1995 Academic Press, Inc. * Tang, T.K., Huang, W., Chang Tang, C., Hsu, M., Cheng, T., and Chen, K. Molecular basis of glucose-6-phosphate dehydrogenase (G6PD) deficiency in three Taiwan aboriginal tribes. Hum.Genet. 95(6):630-632, 1995. Notes: We have investigated glucose-6-phosphate dehydrogenase (G6PD) deficiency in 220 unrelated aboriginal male subjects who belong to three different tribes (Saisiat, Ami, and Yami) in Taiwan. Our results show that the G6PD deficiency rates for Saisiat, Ami, and Yami people are 9.0% (6/67), 6.1% (6/99), and 0% (0/54), respectively. Among these deficiency cases, 4 of 6 (66.7%) Saislat subjects have the 493 A-->G mutation and one carries the 1376 G-->T mutation, whereas, in Ami subjects, we found that four of six (66.7%) affected males have the 592 C-->T mutation and one carries the 493 A-->G mutation. These results contrast with our previous findings for Taiwan Chinese, in whom the 1376 G-->T mutation is the major mutant allele and accounts for 52.3% of the deficiency cases. This is the first report of G6PD deficiency characterized at the DNA level in Taiwan

aboriginal populations. * Tang, T.K., Liu, T., Tang, C.C., and Tam, K. Glucose-6-phosphate dehydrogenase (G6PD) mutations associated with F8C/G6PD haplotypes in Chinese. Blood 85(12):3767-3768, 1995. * Tang, T.K., Chen, H.-L., Huang, C.-S., and Liu, T.-H. Identification of a novel G6PD mutation (G6PD NanKang) and the association of F8C/G6PD haplotypes in Chinese. Blood 86(Suppl 1):134a, 1995. * Washington, E.C., Ector, W., Abboud, M., Ohning, B., and Holden, K. Hemolytic jaundice due to G6PD deficiency causing kernicterus in a female newborn. South.Med.J. 88(7):776-779, 1995. Notes: Glucose-6-phosphate dehydrogenase (G6PD) deficiency is an inherited deficiency of an enzyme necessary to protect the erythrocyte from oxidative stress and hemolysis. Without this enzyme, affected neonates are at risk for acute onset of hemolytic jaundice and severe sequelae, from hearing loss and mild retardation to kernicterus. In some populations, especially in blacks and those of Mediterranean ancestry, the incidence of G6PD deficiency has been reported to be as high as 10% to 14%. We describe a female newborn who had acute onset of hyperbilirubinemia leading to kernicterus in the first week of life. Investigation proved G6PD deficiency. This case suggests a need to screen for this disease or to follow serial bilirubin levels in populations at risk. Type not given in the abstract. Assuem A- until paper obtained. * Xu, W., Westwood, B., Bartsocas, C.S., Malcorra-Azpiazu, J.J., Indr k, K., and Beutler, E. Glucose-6 phosphate dehydrogenase mutations and haplotypes in various ethnic groups. Blood 85:257-263, 1995. Notes: (MS413)(B1003) Mutations that produce glucose-6-phosphate dehydrogenase (G6PD) deficiency have been identified in samples from patients with hemolytic disease in the United States, and in G6PD- deficient samples from Greece, the Canary Islands, the Czech and Slovak Republics, South China, and in samples from the Coriell Cell Repository. Eight new mutations are described. Particularly unusual were a nonsense mutation ("G6PD Georgia"(1284A)), a deletion of six bases ("G6PD Stony Brook"(724-729 del) dal) coding for two amino acids, and a deletion of the invariant dinucleotide ApG at the 3' acceptor splice site in the highly conserved sequence between intron 10 and exon 11 ("G6PD Varnsdorf"). In addition, five new missense point mutations were identified: "G6PD Cleveland"(820A) creates a deduced AA 274 Glu -- > Lys; "G6PD West Virginia"(910T) AA 303 Val --> Phe; "G6PD Fushan"(1004A), AA 335 Ala --> Asp; "G6PD Olomouc"(1141C) AA 381 Leu --> Phe; and "G6PD Praha"(1166G) AA 389 Glu --> Gly All Of the new m * Ackerman, Z., Ablin, J., and Shouval, D. Active immunization against hepatitis A is now warranted in glucose-6-phosphate dehydrogenase-deficient subjects. Am.J.Gastroenterol. 91(2):413, 1996. * Bayoumi, R.A., Nur-E-Kamal, M.S.A., Tadayyon, M., Mohamed, K.K.A., Mahboob, B.H., Qureshi, M.M., Lakhani, M.S., Awaad, M.O., Kaeda, J., Vulliamy, T.J., and Luzzatto, L. Molecular characterization of erythrocyte glucose-6-phosphate dehydrogenase deficiency in Al-Ain District, United Arab Emirates. Hum.Hered. 46(3):136-141, 1996. Notes: In a cross-sectional study, the activity, electrophoretic mobility and genotypes of glucose-6-phosphate dehydrogenase

(G6PD) were determined among healthy, UAE national school boys from Al-Ain District in the United Arab Emirates. The prevalence of G6PD deficiency in this population sample was 11%, The majority of G6PD-deficient subjects were descendants of Omani, Baluchi or Yemeni migrants. Of 18 deficient subjects, 16 had an enzyme activity of < 10% of normal while 2 had an activity of just above 10%, Electrophoresis was performed on 166 samples and showed that, apart from deficient samples, all had the normal mobility of G6PD type B. Of the 18 deficient subjects, 14 had the B type mobility of G6PD Mediterranean and 4 had the A type mobility of G6PD A-. Genotyping demonstrated that 10 had the Mediterranean mutation while 3 had the A-mutation, consistent with their electrophoretic mobility, Another 3 had the G6PD Aures mutation, recently described as polymorphic in Algeria and Spain. The mutations * Beutler, E., Vulliamy, T., and Luzzatto, L. Hematologically important mutations: Glucose-6-phosphate dehydrogenase. Blood Cells Mol.Dis. 22:49-56, 1996. Notes: (MS469) (B1057). * Corey, S.J. and Beutler, E. Clinical, genetic and biochemical features of G-6-PD West Virginia. In preparation , 1996. Notes: (MS468)Submitted Am.J.Hematol. by S. Corey 14 Feb 1996. * G"mez-Gallego, F., Garrido-Pertierra, A., Mason, P.J., and Bautista, J.M. Unproductive folding of the human G6PD-deficient variant A-. FASEB J. 10(1):153-158, 1996. Notes: Human glucose-6-phosphate dehydrogenase (G6PD) deficiency almost invariably results from the presence of missense mutations in the X-Linked gene encoding G6PD. The common African deficient variant G6PD A(-) differs from the normal G6PD B by two amino acid substitutions. Only one of these mutations is found on its own, resulting in the nondeficient variant G6PD A, Deficiency is always associated with decreased G6PD activity in red cells, leading to a variety of clinical manifestations, A group of deficient variants, including A(-), have near-normal affinity for the substrates G6P and NADP. In these cases, deficiency is caused by a decreased number of catalytically active molecules per cell due to intracellular instability of the mutated G6PD, although the mechanism for this in vivo instability is unknown. Here we report that in vitro folding of the A(-) variant mainly renders partially folded polypeptides that do not undergo the dimerization required for activity, Under the same conditions, the nonde * Huang, C.-S., Hung, K.L., Huang, M.J., Li, Y.C., Liu, T.H., and Tang, T.K. Neonatal jaundice and molecular mutations in glucose-6-phosphate dehydrogenase deficient newborn infants. Am.J.Hematol. 51(1):19-25, 1996. Notes: Molecular mutations of the glucose-6-phosphate dehydrogenase (GGPD) gene and clinical manifestations of neonatal jaundice in 112 male and 50 female Chinese neonates with G6PD deficiency were studied, In the 112 males, the nucleotide (nt) 1376 (G-->T) mutation was the dominant type (50.0%), followed by nt 1388 (G-- >A) (16.1%), nt 493 (A-->G) (8.0%), nt 1024 (C-->T) (6.2%), nt 95 (A-->G) (5.4%), nt 392 (G-->T) (1.8%), nt 487 (G-->A) (1.8%), nt 871 (G-->A) (0.9%), and nt 1360 (C-->T) (0.9%). The nt 871 variant has not been reported in Taiwan before, The occurrence rates for nt 1376, nt 1388, nt 493, nt 95, and nt 1024 mutations in the 50 females were 44.0%, 18.0%, 12.0%, 6.0%, and 6.0%, respectively, The type of G6PD mutation in 10 male and 7 female neonates has not been identified yet. Although

G6PD deficient neonates had higher frequency of phototherapy than G6PD normal neonates in both sexes, a significant difference in the prevalence of hyperbilirubinemia (peak bilirubin greater than or equal to 1 * Huo, T.I., Wu, J.C., Chiu, C.F., and Lee, S.D. Severe hyperbilirubinemia due to acute hepatitis a superimposed on a chronic hepatitis B carrier with glucose-6-phosphate dehydrogenase deficiency. Am.J.Gastroenterol. 91(1):158-159 ----, 1996. Notes: Taiwan is an endemic area for hepatitis A and B virus infections; nearly 90% of adults have serological markers for either virus, Glucose-6-phosphate dehydrogenase (G6PD) deficiency is also common, ranging from 2% to 10%, We report the case of a 36-yr-old chronic HBV male carrier with G6PD deficiency who developed acute viral hepatitis A with severe hyperbilirubinemia and intravascular hemolysis, The hemolysis was in all likelihood the result of recent exposure to sulfa drugs, Fulminant hepatitis was the initial impression, because the peak serum total bilirubin concentration was alarmingly high, at 85.4 mg/dl, Exchange plasmapheresis with fresh frozen plasma was performed, and various laboratory studies gradually returned to near normal over the next 3 wk, The patient made an uneventful recovery 1 month after admission. * Lee, D.H., Warkentin, T.E., Neame, P.B., and Ali, M.A.M. Acute hemolytic anemia precipitated by myocardial infarction and pericardial tamponade in G6PD deficiency. Am.J.Hematol. 51(2):174-175, 1996. * Meloni, G. and Meloni, T. Glyburide-induced acute haemolysis in a G6PD-deficient patient with NIDDM. Br.J.Haematol. 92(1):159-160, 1996. Notes: In a 61-year-old man with glucose-6-phosphate dehydrogenase (G6PD) deficiency and poorly controlled non-insulin-dependent diabetes mellitus, an episode of acute haemolysis occurred after the administration of glyburide (glibenclamide). Erythrocyte fragmentation, with haemoglobin condensation zones next to clear zones, was observed on peripheral blood smears. Since autoimmune haemolysis was excluded on the basis of laboratory data, dehydrogenase (G6PD) deficiency and poorly controlled acute haemolysis was ascribed to G6PD deficiency. * Miwa, S. and Fujii, H. Molecular basis of erythroenzymopathies associated with hereditary hemolytic anemia: Tabulation of mutant enzymes. Am.J.Hematol. 51(2):122-132, 1996. Notes: Molecular abnormalities of erythroenzymopathies associated with hereditary hemolytic anemia have been determined by means of molecular biology. Pyruvate kinase (PK) deficiency is the most common and well-characterized enzyme deficiency in the glycolytic pathway, and it causes hereditary hemolytic anemia. To date, 47 gene mutations have been identified, We identified one base deletion, one splicing mutation, and six distinct missense mutations in 12 unrelated families with a homozygous PK deficiency. Mutations located near the substrate or fructose-1,6diphosphate binding site may change the conformation of the active site, resulting in a drastic loss of activity and severe clinical symptoms. Glucose-6-phosphate dehydrogenase (G6PD) deficiency is the most common metabolic disorder, and it is associated with chronic hemolytic anemia and/or drug- or infection-induced acute hemolytic attack, An estimated 400 million people are affected worldwide. The mutations responsible for about 78 variants have bee

* Naylor, C.E., Rowland, P., Basak, A.K., Gover, S., Mason, P.J., Bautista, J.M., Vulliamy, T.J., Luzzatto, L., and Adams, M.J. Glucose 6-phosphate dehydrogenase mutations causing enzyme deficiency in a model of the tertiary structure of the human enzyme. Blood 87(7):2974-2982, 1996. Notes: Human glucose 6-phosphate dehydrogenase (G6PD) has a particularly large number of variants resulting from point mutations; some 60 mutations have been sequenced to date. Many variants, some polymorphic, are associated with enzyme deficiency. Certain variants have severe clinical manifestations; for such variants, the mutant enzyme almost always displays a reduced thermal stability. A homology model of human G6PD has been built, based on the three-dimensional structure of the enzyme from Leuconostoc mesenteroides. The model has suggested structural reasons for the diminished enzyme stability and hence for deficiency. It has shown that a cluster of mutations in exon 10, resulting in severe clinical symptoms, occurs at or near the dimer interface of the enzyme, that the eight-residue deletion in the variant Nara is at a surface loop, and that the two mutations in the A- variant are close together in the three-dimensional structure. * Roos, D., van Zwieten, R., Wijnen, J.T., Pronk-Admiraal, C.J., Weening, R.S., Ploem, J.E., Beutler, E., and Khan, P.M. Molecular basis and enzymatic properties of glucose-6-phosphate dehydrogenase Volendam, leading to chronic nonspherocytic anemia, granulocyte dysfunction and increased susceptibility to infections. In preparation , 1996. Notes: (MS465). * Vlachos, A., Westwood, B., and Beutler, E. G6PD Mt. Sinai. A new hemolytic variant. In preparation , 1996. Notes: (MS425) G6PD Mt.Sinai.