Effects of flavonoids on xanthine oxidation as well as on cytochrome c reduction by milk xanthine oxidase.
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منابع مشابه
Effects of flavonoids on xanthine oxidation as well as on cytochrome c reduction by milk xanthine oxidase.
That flavonoids inhibit xanthine oxidase from cow milk was confirmed by measuring oxygen consumption with an oxygen electrode. In contrast, flavonoids did not inhibit glucose oxidase, another oxygen consuming enzyme. Among the flavonoids tested, quercetin, kaempferol, myricetin, chrysin, quercitrin, and morin were potent inhibitors of xanthine oxidase; their inhibition rates (%) were 80, 70, 69...
متن کاملThe reduction of cytochrome c by milk xanthine oxidase.
The reduction of cytochrome c by xanthine oxidase and the competitive inhibition of this process by carbonic anhydrase and by myoglobin have been studied by kinetic and by equilibrium binding methods. Carbonic anhydrases isolated from bovine and from human erythrocytes differed strikingly in their ability to inhibit competitively the reduction of cytochrome c. The KS for cytochrome c was a func...
متن کاملTHE REDUCTION OF CYTOCHROME c BY XANTHINE OXIDASE
A number of substances such as oxygen, dyes, and nitrate can act as hydrogen acceptors for xanthine oxidase (1). It has now been found that cytochrome c is also reduced by this system. Since only one other enzyme has been isolated which reduces cytochrome c (2), it was of interest to study the reaction, particularly since Ball (3) has indicated that xanthine oxidase is a flavoprotein. The activ...
متن کاملThe reduction of cytochrome c by hypoxanthine and xanthine oxidase.
Ball, E. G. (1939a). J. biol. Chem. 128, 51. Ball, E. G. (1939b). Cold Spr. Harb. Sym. quant. Biol. 7, 100. Ball, E. G. (1946). J. gen. Phy8iol. 29, 413. Corran, H. S., Dewan, J. G., Gordon, A. H. & Green, D. E. (1939). Biochem. J. 38, 1694. Dixon, M. (1938). Enzymologia, 5, 198. Dixon, M. & Keilin, D. (1936). Proc. roy. Soc. B, 119, 159. Green, D. E., Knox, W. E. & Stumpf, P. K. (1941). J. bio...
متن کاملXanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid as follows
The enzyme is well-suited to carry out the catalysis of these oxidative reactions, containing as it does four redox-active sites: molybdenum, flavin adenine dinucleotide (FAD) and a pair of iron-sulfur centers of the ferredoxin type (Fe2S2). The purine substrates interact with the enzyme at the molybdenum site of xanthine oxidase and oxygen at the flavin site. The two metabolic reactions above ...
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ژورنال
عنوان ژورنال: Journal of Nutritional Science and Vitaminology
سال: 1986
ISSN: 0301-4800,1881-7742
DOI: 10.3177/jnsv.32.635