Diperoxovanadate participates in peroxidation reactions of H2O2 in presence of abundant catalase

被引：15

作者：

Rao, AVS ^{[1
]}

Ravishankar, HN ^{[1
]}

Ramasarma, T ^{[1
]}

机构：

[1] Indian Inst Sci, Dept Biochem, Bangalore 560012, Karnataka, India

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS | 1998年 / 1381卷 / 02期

关键词：

vanadate; catalase; H2O2; diperoxovanadate;

D O I：

10.1016/S0304-4165(98)00038-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Vanadate forms a stable complex with H2O2 at pH 7.0 in competition with catalase and the product, diperoxovanadate, resists scavenger action of catalase. Diperoxovanadate can act as a substrate in a H2O2-user reaction, horseradish peroxidase and can take the place of H2O2 far more effectively in oxidatively inactivating glyceraldehyde-3-phosphate dehydrogenase. By forming peroxo-complexes vanadate can provide a way of preserving cellular H2O2 in presence of abundant catalase and make it available for its functions. (C) 1998 Elsevier Science B.V. All rights reserved.

引用

页码：249 / 255

页数：7

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