Diaphorase (coenzyme factor)

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The relative essentiality of the antioxidative function of coenzyme Q--the interactive role of DT-diaphorase.

This paper will address two aspects regarding the antioxidative role of coenzyme Q (CoQ): (1) Is the antioxidant function of CoQ primary or secondary (coincidental), i.e. was this molecule selected during evolution to function primarily as an essential functional component of the mitochondrial electron transfer chain and oxidative phosphorylation processes, is its antioxidative capability merel...

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The role of DT-diaphorase in the maintenance of the reduced antioxidant form of coenzyme Q in membrane systems.

The experiments reported here were designed to test the hypothesis that the two-electron quinone reductase DT-diaphorase [NAD(P)H:(quinone-acceptor) oxidoreductase, EC 1.6.99.2] functions to maintain membrane-bound coenzyme Q (CoQ) in its reduced antioxidant state, thereby providing protection from free radical damage. DT-diaphorase was isolated and purified from rat liver cytosol, and its abil...

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Triphosphopyridine Nucleotide Diaphorase from Wheat Germ.

11. KREBS, H. A. and HENSELEIT, K. Untersuchungen iiber die harnstoffbildung im tierkorper. Zeit. physiol. Chem. 210: 33. 1932. 12. McELROY, W. D. and GLASS, H. B. Amino acid Metabolism. Pp. 300-320. Johns Hopkins Press, Baltimore 1955. 13. MUELLER, G. C., QUINN, E. M. and RUECKERT, R. R. The formation of 1-phosphoerythrulose-4-C" by homogenates of Swiss chard leaves. Arch. Biochem. Biophys. 55...

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FAD-Dependent NAD(P)H Diaphorase

A newly discovered human diaphorase, designated diaphorase-4, which accounts for a major part of the diaphorase activity of most tissues but does not occur in erythrocytes, is described. In contrast with other human diaphorases, it is dependent on FAD for activity after electrophoresis, inhibited by low concentrations of dicoumarol and shows a marked affinity for Cibacron Blue. The molecular we...

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The Histochemical Localization of Triphosphopyridine Nucleotide Diaphorase

A histochemical method is described for the localization of triphosphopyridine nucleotide diaphorase using a recently synthesized tetrazolium salt (Nitro-BT). By virtue of the favorable histochemical properties of this reagent, it has been possible to demonstrate that whereas DPN diaphorase is usually restricted to the mitochondria, the TPN diaphorase activity of corresponding cells was distrib...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1939

ISSN: 0306-3283

DOI: 10.1042/bj0330613