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dc.contributor.authorSrivastava, P K-
dc.contributor.authorSingh, D S-
dc.identifier.issn0975-0959 (Online); 0301-1208 (Print)-
dc.description.abstractNADP+- linked isocitrate dehydrogenase (E.C. has been purified to homogeneity from germinating pea seeds. The enzyme is a tetrameric protein (mol wt. about 146,000) made up of apparently identical monomers (subunit mol wt, about 36,000). Thermal in activation of purified enzyme at 45° and 50°C shows simple first order kinetics. The enzyme shows optimum activity at pH range 7.5-8. Effect of substrate [S] on enzyme activity at different pH (6.5-8) suggests that the proton behaves formally as an "uncompetitive inhibitor". A basic group of the enzyme (site) is protonated in this pH range in the presence of substrate only, with a pKa equal to 6.78. On successive dialysis against EDTA and phosphate Buffer, pH 7.8 at O°C, yields an enzymatically inactive protein showing kinetics of thermal inactivation identical to the untreated (native) enzyme. Maximum enzyme activity is observed in presence of Mn2+ and Mg2+ ions (3.75 mM). Addition of Zn2+, Cd2+, C02+ and Ca2+ ions brings about partial recovery. Other metal ions Fe2+, Cu2+ and Ni2+ are ineffective.en_US
dc.publisherNISCAIR-CSIR, Indiaen_US
dc.rights CC Attribution-Noncommercial-No Derivative Works 2.5 Indiaen_US
dc.sourceIJBB Vol.38(5) [October 2001]en_US
dc.titleIsolation and characterization of NADP+ -linked isocitrate dehydrogenase of germinating pea seeds (Pisum sativum)en_US
Appears in Collections:IJBB Vol.38(5) [October 2001]

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