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- W2040231314 abstract "Abstract Cytochrome P-450 has been partially purified from uninduced rat liver to a specific content of 9.6 nmoles/mg protein, and contains no cytochrome b5 or NADPH-cytochrome c reductase. Microsomes were solubilized by Emalgen 913 followed by ammonium sulfate precipitation and column chromatography on DEAE-cellulose and calcium phosphate gel. The cytochrome P-450 is catalytically active when reconstituted with lipid and NADPH-cytochrome c reductase for hydroxylation of benzo[a]pyrene." @default.
- W2040231314 created "2016-06-24" @default.
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- W2040231314 date "1978-03-01" @default.
- W2040231314 modified "2023-09-23" @default.
- W2040231314 title "Isolation and partial purification of cytochrome P-450 from uninduced rat liver" @default.
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- W2040231314 doi "https://doi.org/10.1016/0006-291x(78)91624-8" @default.
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