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• W2028924242 abstract "NADPH-cytochrome P-450 reductase with capacity to support cytochrome P-450-dependent drug metabolism and to reduce artificial electron acceptors has been purified to apparent homogeneity by solubilization with Renex 690 and chromatography on DEAE-Sephadex, Agarose and QAE-Sephadex. The purified protein migrates as a single band on native and SDS-polyacrylamide gel electrophoresis, exhibits a minimum molecular weight of 80,000 daltons and contains 1 molecule each of FAD and FMN per 80,000 molecular weight. The specific activity for cytochrome c as electron acceptor is 48.8 μmoles per min and for substrate hydroxylation of benzphetamine measured as NADPH oxidation in the presence of cytochrome P-450 and phosphatidylcholine is 2.5 μmoles per min." @default.
• W2028924242 created "2016-06-24" @default.
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• W2028924242 date "1975-04-01" @default.
• W2028924242 modified "2023-10-16" @default.
• W2028924242 title "Preparation of homogeneous NADPH-cytochrome P-450 reductase from rat liver" @default.
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• W2028924242 doi "https://doi.org/10.1016/0006-291x(75)90644-0" @default.
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