Papers by Michael Banyard
British Journal of Cancer, 1984
A monoclonal antibody was prepared against DIDS, an inhibitor of anion transport, and used to com... more A monoclonal antibody was prepared against DIDS, an inhibitor of anion transport, and used to compare the occurrence and distribution of DIDS-binding sites of tumorigenic and non-tumorigenic human somatic-cell hybrids. The monoclonal antibody (E8) was produced by the fusion of the mouse myeloma (NS-1) with mouse spleen cells and is of the IgGI subclass. The apparent half-saturation of DIDS for HEp-2 cells is 16yM and the reaction is rapid. The number of binding sites on tumorigenic and non-tumorigenic hybrid cells was the same. The DIDS-binding protein occurs homogeneously on all cells, a characteristic which distinguishes it from the possible tumour antigen recognised by the M/27 monoclonal antibody.
Molecular and Cellular Biochemistry, 1982
Gentle procedures are described for the fractionation of bovine tear fluid by a combination of ce... more Gentle procedures are described for the fractionation of bovine tear fluid by a combination of centrifugation, salt precipitation, gel filtration and ion exchange chromatography. Fractions are examined by gel electrophoretic immunological methods. Reference patterns are compiled and compared with bovine milk and serum patterns. Properties of some of th components are determined. Lactoferrin is isolated in two separate, but closely related, fractions. An acidic protein with a molecular weight of 23 000 daltons, is also isolated. Distinct heterogeneity is observed between individual animals, suggestive of a genetic polymorphism. A method is presented for the determination of the antibacterial activity of tear fluid and its fractions.
Biochemical and Biophysical Research Communications, 1986
The Journal of Membrane Biology, 1987
Four monoclonal antibodies against the calcium ATPase in sarcoplasmic reticulum (SR) of rabbit fa... more Four monoclonal antibodies against the calcium ATPase in sarcoplasmic reticulum (SR) of rabbit fast-twitch skeletal muscle were characterized using SDS-PAGE, Western blots and immunofluorescence. The ultrastructural distribution of the antigens was determined using post-embedding immunolabeling. The antibodies recognized the calcium ATPase in the SR but not in transverse (T-) tubule or plasma membranes. The antibody, D12, had the same binding affinity for the calcium ATPase from fast-twitch (rabbit sternomastoid) and slow-twitch (rabbit soleus) fibers and the affinity fell by 30% after fixation for electron microscopy in both types of muscle fiber. Ultrastructural studies revealed that the density of D12 antibody binding to the terminal cisternae membrane of extensor digitorum Iongus (edl) and sternomastoid fibers was on average seven times greater than in the slow-twitch soleus and semimembranosus fibers. Since the affinity of the ATPase for the antibody was the same in SR from fast-and slow-twitch muscles, the concentration of calcium ATPase in the terminal cisternae membrane of fast-twitch fibers was seven times greater than in slow-twitch fibers. This conclusion was supported by the fact that the concentration of calcium ATPase in light SR membranes was six times greater in SR from fast-twitch fibers than in SR from slow-twitch fibers. The results provide strong evidence that the different calcium accumulation rates in mammalian fast-and slow-twitch muscles are due to different concentrations of calcium ATPase molecules in the SR membrane.
Australian veterinary journal, 2013
Australian veterinary journal, 2016
Australian Journal of Experimental Biology and Medical Science, 1985
An cryihroo'iv staloglycoprotoiii common aniigcn has hccn idciilificd by a monoclonal antibody. T... more An cryihroo'iv staloglycoprotoiii common aniigcn has hccn idciilificd by a monoclonal antibody. The antigen recognised by the JCS-2 antibody was determined by immunopr«:ipitauon, Western blotting and partial amino acid scquencinti:. Wciitcrn blot analysis of human erythrocyie gho?.t membranes separated on sodium dodecyl sulphate polyacrylamide gel electrophoresis shows thai the sialoglycoprotcin i;ommnn aniigcn occurs on the alpha, beta, gamma and delta sialoglytoproteins, eilher in then monomenc or dimrric form and a^ the heterodimer in the case of alpha and delta. The ^V terminal sequence of (he antigen prqiaml b>' immunoafflniiy chromatography of the Triion-\IOO extract of human erythroc>tc ghosts shows ihe first 9 residues to be identical lo the known sequence of the MN blood group glycoproteins. The common epitope on the sialoglycoproieim resides on the oligo&accharide and contains sialic acid.
Australian veterinary journal, 2013
Molecular and Cellular Biochemistry, 1982
Gentle procedures are described for the fractionation of bovine tear fluid by a combination of ce... more Gentle procedures are described for the fractionation of bovine tear fluid by a combination of centrifugation, salt precipitation, gel filtration and ion exchange chromatography. Fractions are examined by gel electrophoretic and immunological methods. Reference patterns are compiled and compared with bovine milk and serum patterns. Properties of some of the components are determined. Lactoferrin is isolated in two separate, but closely related, fractions. A nacidic protein with a molecular weight of 23 000 daltons, is also isolated. Distinct heterogeneity is observed between individual animals, suggestive of a genetic polymorphism. A method is presented for the determination of the antibacterial activity of tear fluid and its fractions.
Biochemical and Biophysical Research Communications, 1986
Uploads
Papers by Michael Banyard