Rao, Aparna VS and Ravishankar, HN and Ramasarma, T (1998) Diperoxovanadate participates in peroxidation reactions of H2O2 in presence of abundant catalase. In: Biochimica et Biophysica Acta (BBA) - General Subjects, 1381 (2). pp. 249-255.
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Abstract
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
Item Type: | Journal Article |
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Publication: | Biochimica et Biophysica Acta (BBA) - General Subjects |
Publisher: | Elsevier Science |
Additional Information: | Copyright of this article belongs to Elsevier Science. |
Keywords: | vanadate;catalase;H2O2;diperoxovanadate. |
Department/Centre: | Division of Biological Sciences > Biochemistry |
Date Deposited: | 20 Mar 2009 06:31 |
Last Modified: | 19 Sep 2010 05:01 |
URI: | http://eprints.iisc.ac.in/id/eprint/18399 |
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