Literature DB >> 6912071

Vanadate-stimulated NADH oxidation in plasma membrane.

T Ramasarma, W C MacKellar, F L Crane.   

Abstract

The rate of NADH oxidation with oxygen as the acceptor is very low in mouse liver plasma membrane and erythrocyte membrane. When vanadate is added, this rate is stimulated 10- to 20-fold. The absorption spectrum of vanadate does not change with the disappearance of NADH. The reaction is inhibited by superoxide dismutase, and there is no activity under an argon atmosphere. This indicates that oxygen is the electron acceptor and the reaction is mediated by superoxide. The vanadate stimulation is not limited to plasma membrane. Golgi apparatus and endoplasmic reticulum show similar increase in NADH oxidase activity when vanadate is added. The endomembranes have significant vanadate-stimulated activity with both NADH and NADPH. The vanadate-stimulated NADH oxidase in plasma membrane is inhibited by compounds, which inhibit NADH dehydrogenase activity: catechols, anthracycline drugs and manganese. This activity is stimulated by high phosphate and sulfate anion concentrations.

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Year:  1981        PMID: 6912071     DOI: 10.1016/0005-2736(81)90275-3

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  13 in total

1.  Decavanadate interacts with microsomal NADH oxidation system and enhances cytochrome c reduction.

Authors:  T Ramasarma; Aparna V S Rao
Journal:  Mol Cell Biochem       Date:  2006-01       Impact factor: 3.396

2.  A vanadate-stimulated NADH oxidase in erythrocyte membrane generates hydrogen peroxide.

Authors:  S Vijaya; F L Crane; T Ramasarma
Journal:  Mol Cell Biochem       Date:  1984-06       Impact factor: 3.396

3.  Vanadium induced hemolysis of vitamin E deficient erythrocytes in Hepes buffer.

Authors:  T Hamada
Journal:  Experientia       Date:  1994-01-15

4.  In vivo insulin resistance in streptozotocin-diabetic rats--evidence for reversal following oral vanadate treatment.

Authors:  O Blondel; D Bailbe; B Portha
Journal:  Diabetologia       Date:  1989-03       Impact factor: 10.122

5.  Stimulation of NADH oxidation by xanthine oxidase and polyvanadate in presence of some dehydrogenases and flavin compounds.

Authors:  K Penta; S Gullapalli; M Rau; T Ramasarma
Journal:  Mol Cell Biochem       Date:  1991-09-18       Impact factor: 3.396

6.  Multiple reactions in vanadyl-V(IV) oxidation by H2O2.

Authors:  H N Shankar; T Ramasarma
Journal:  Mol Cell Biochem       Date:  1993-12-08       Impact factor: 3.396

7.  Vanadate-stimulated NADH oxidation in microsomes.

Authors:  M Rau; M S Patole; S Vijaya; C K Kurup; T Ramasarma
Journal:  Mol Cell Biochem       Date:  1987-06       Impact factor: 3.396

8.  NADH-dependent polyvanadate reduction by microsomes.

Authors:  M S Patole; C K Kurup; T Ramasarma
Journal:  Mol Cell Biochem       Date:  1987-06       Impact factor: 3.396

9.  Characterization of vanadate-dependent NADH oxidation stimulated by Saccharomyces cerevisiae plasma membranes.

Authors:  L A Minasi; G R Willsky
Journal:  J Bacteriol       Date:  1991-01       Impact factor: 3.490

10.  Characterization of oxygen free radicals generated during vanadate-stimulated NADH oxidation.

Authors:  P Kalyani; S Vijaya; T Ramasarma
Journal:  Mol Cell Biochem       Date:  1992-04       Impact factor: 3.396

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