Sanjay Mishra

IFTM Universiry Moradabad, Biotechnolgy, Faculty Member

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Dr. Sanjay Mishra (Ph.D; FSAB; FICN) is currently working as an independent researcher in the capacity of Professor & Dean, School of Biotechnology, IFTM University, Moradabad India. In 1993, he was appointed as Scientist at the Division of Biochemistry and Molecular Biology, Central Institute of Medicinal and Aromatic Plants, India. In 1997, he was appointed as Lecturer at the Department of Biochemistry, University of Lucknow, Lucknow, Uttar Pradesh, India. In 1998, he was appointed as Visiting Researcher at the Department of Applied Microbiology, National Institute of Bioscience and Human Technology, Tsukuba, Japan. In 2000, he was appointed as Post Doctoral Fellow at the Boston Biomedical Research Institute, Watertown, Massachusetts, USA. In 2001, he was appointed as Research Associate at the Department of Biological Sciences, Kent State University, Ohio, USA. In 2003, he was appointed as Assistant Professor at the Shri Ram Murti Smarak College of Engineering and Technology, Bareilly, India. In 2006, he was appointed as Assistant Professor at the College of Engineering and Technology, Institute of Foreign Trade and Management Campus, India. In 2007, he was appointed as Professor at the Department of Biotechnology, College of Engineering and Technology, Institute of Foreign Trade and Management Campus, India.

Dr. Sanjay Mishra received his B.Sc. in Biology in 1982 at University of Lucknow, Lucknow, Uttar Pradesh, India. He got M.Sc. in Biochemistry in 1984 from University of Lucknow, Lucknow, Uttar Pradesh, India. Dr. Sanjay Mishra obtained Ph.D. from University of Lucknow, Lucknow, Uttar Pradesh, India in 1993 in Biochemistry and Biotechnology.

Dr. Sanjay Mishra’s current research interests are Animal Biochemistry and Biotechnology, Cancer Biology, Immunology and Medicine, Tuberculosis, Reproductive Biology, Enzymology and Protein Engineering, Bioinformatics and Biomedical Engineering.

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Dynamics of Tropane Alkaloids in Duboisia myoporoides Leaf During Development

Journal of Herbs, Spices & Medicinal Plants, 1997

AGRIS record. Record number, US1997053481. Titles, Dynamics of tropane alkaloids in Duboisia myop... more

Direct Fluorometry of Phase-Extracted Tryptamine-Based Fast Quantitative Assay ofl-Tryptophan Decarboxylase fromCatharanthus roseusLeaf

Analytical Biochemistry, 1998

roseus leaf as the enzyme source, it should be equally applicable to other plant and nonplant sou... more roseus leaf as the enzyme source, it should be equally applicable to other plant and nonplant sources. The An assay for the enzyme L-tryptophan decarboxylase (TDC; EC 4.1.1.28) is described. It is based on direct merits and precautions of the protocol have been discussed. ᭧ 1998 Academic Press fluorometry of the enzymatic reaction product (tryptamine) selectively recovered in ethyl acetate from the reaction mixture. Catalytically formed tryptamine from tryptophan in the incubation mixture is selec-Tryptophan decarboxylase (TDC; 2 EC 4.1.1.28, fortively (free from tryptophan) physically separated as merly EC 4.1.1.27) catalyzes pyridoxal-phosphateethyl acetate solution under basic (pH ¢ 11) condidependent irreversible decarboxylation of L-tryptotions and subjected to direct fluorescence measurephan into tryptamine. The catalytic reaction follows ment in the organic solvent using a spectrofluorothe pyroquinoline-quinone mechanism. The protoalmeter with excitation and emission wavelengths of kaloid tryptamine, thus produced, becomes a commit-280 and 350 nm, respectively. Tryptamine production rate was quantitated from the luminescence response ted metabolic precursor for the synthesis of a vast numcurve of tryptamine drawn under similar extraction ber of indole alkaloids encountered in higher plants. and measurement conditions. Luminescence calibra-These include some of the most important pharmaphytion curves were drawn for tryptamine in aqueous tochemicals produced by genera like Cinchona, Cathar-(water or buffer system) as well as in organic solvent anthus, Tabernaemontana, Peganum, Rauwolfia, etc. as recovered from the varied aqueous solution condi-(1, 2). Several lines of observations imply that TDC is tions including those similar to the enzyme incubaone of the key regulators in the synthesis and accumution mixture. The luminescence calibration graphs lation of the alkaloids in different producer plants as were linear for at least 0.5 to 10 mM tryptamine. The well as tissue types. Briefly, some of the supportive examination of interassay variations and the comparobservations are tryptamine as nonubiquitous in ative magnitude of fluorescence response allowed to higher plants and its significant levels observed only infer that a satisfactory and sufficient sample lumiin plants and tissues engaged in the biosynthesis of nescence response was retained under the varied conthe indolyl secondary metabolites; increased formation ditions including those akin to the enzymatic assay of tryptamine and of indole alkaloids preceded by inmixture, allowing adaptation of the fluorometry for crease in TDC activity in germinating seedlings and the TDC activity quantitation. The assay was found to suspension cultures of Catharanthus roseus and Cinfollow the proportionality principle of product formachona ledgeriana (3, 4); a strong correlation of ention with respect to catalytic reaction time as well hanced TDC activity and accumulation of harman alkaas protein concentration in the assay mixture using loids and serotonin in Peganum harmala suspension Catharanthus roseus leaf crude homogenate as well cultures (5); de novo synthesis and a dramatic increase as the enzyme preparation at different states of puin TDC activity after transfer of C. roseus and C. ledrity. The rate of tryptamine formation under the catageriana suspension cultures from growth medium into lytic conditions was linear for at least 1 h at 30ЊC. Though the assay has been demonstrated to use the C.

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