Inosine 5′-phosphate dehydrogenase of pea seeds

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منابع مشابه

Inosine 5'-phosphate dehydrogenase of pea seeds.

The work described in this paper was carried out as part of the joint research programme of the Division of Food Preservation, C.S.I.R.O., and of the Botany School, University of Sydney. The authors wish to express their indebtedness to Miss S. K. Harris and Miss N. J. Eames for technical assistance; and to Dr J. R. Vickery, Chief, Division of Food Preservation, and Professor R. L. Crocker, Bot...

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Inosine 5 0 - Monophosphate Dehydrogenase

I. Overview of IMPDH A. Protein Structures II. Medicinal Applications of IMPDH Inhibitors A. IMP Analogs B. NAD Analogs C. Natural Product Inhibitors D. Novel Synthetic Inhibitors III. Kinetic Mechanism and Substrate Interactions A. Case Studies 1. Tritrichomonas foetus IMPDH 2. Escherichia coli IMPDH 3. Human IMPDH B. Ligand Binding 1. IMP Binding Site 2. NAD Binding Site IV. Chemical Mechanis...

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Purification and Characterization of Glucose-6-Phosphate Dehydrogenase from Pigeon Pea (Cajanus cajan) Seeds

Glucose-6-phosphate dehydrogenase has been purified from pigeon pea (Cajanus cajan) seeds and subjected to characterization. The enzyme was purified 123.69 fold with a yield of 21.37% by ammonium sulphate fractionation, PEG-4000 precipitation, CM cellulose column chromatography and DEAE cellulose column chromatography. The catalytically active enzyme is a dimer of 113 KDa with a subunit molecul...

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Biochemically Directed Therapy of Leukemia with Tiazofurin, a Selective Blocker of Inosine 5'-Phosphate Dehydrogenase Activity1

Tiazofurin (2-/3-i>-ribofuranosylthiazole-4-carboxamide, NSC 286193), a selective inhibitor of the activity of IMP dehydrogenase (EC 1.1.1.205), the rate-limiting enzyme of de novo GTP biosynthesis, provided in end stage leukemic patients a rapid decrease of IMP dehydrogenase activity and GTP concentration in the blast cells and a subsequent decline in blast cell count. Sixteen consecutive pati...

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Partial purification, properties and regulation of inosine 5'phosphate dehydrogenase in normal and malignant rat tissues.

IMP dehydrogenase (EC 1.2.1.14) was purified 180-fold from rat liver and from the transplantable rat hepatoma 3924A. The enzymes from the two sources were apparently identical; they exhibited hyperbolic saturation kinetics and an ordered, sequential mechanism, and were subject to inhibition by a number of purine nucleotides. Km values for the substrates, IMP and NAD+, were 12 and 24 micrometer ...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1961

ISSN: 0306-3283

DOI: 10.1042/bj0790147