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- W1932085378 abstract "The activity of purified bovine adrenodoxin reductase was studied. The activity of the enzyme in reducing 2,6,-dichlorophenolindophenol was maximal at about pH 6.5. The enzyme activity was affected by the ionic strength of the medium. Low concentrations of the cofactor FAD restored much of the activity of enzyme preparations which reduced dichlorophenolindophenol slowly. Higher concentrations of FAD inhibited both this reduction by adrenodoxin reductase and steroid hydroxylation by extracts of adrenal mitochondrial protein. These inhibitory effects may be the result of the reduction (with subsequent autoxidation under aerobic conditions) of FAD by NADPH in the presence of adrenodoxin reductase. The latter effect was demonstrated under anaerobic conditions. Some possible reasons for and implications of the observations are discussed." @default.
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- W1932085378 date "2009-01-12" @default.
- W1932085378 modified "2023-09-23" @default.
- W1932085378 title "ADRENODOXIN REDUCTASE, THE FLAVOPROTEIN COMPONENT OF ADRENAL MITOCHONDRIAL STEROID HYDROXYLASES:" @default.
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- W1932085378 doi "https://doi.org/10.1111/j.1399-3011.1974.tb02379.x" @default.
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