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- W2068124326 abstract "Abstract Cytochrome P-450 from rat lung microsomes has been solubilized and purified 8-fold by using affinity chromatography on an ω-amino- n -octyl derivative of Sepharose 4B. The purified fraction was free of cytochrome b 5 and NADPH-cytochrome c reductase and showed spectral characteristics similar to those of lung microsomal cytochrome P-450. When combined with NADPH-cytochrome c reductase partially purified from liver microsomes, the cytochrome P-450 fraction supported the hydroxylation of benzo (α)pyrene and the activity was proportional to the content of the hemoprotein. No absolute requirement for phosphatidylcholine was found." @default.
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- W2068124326 date "1975-06-01" @default.
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- W2068124326 title "Solubilization and partial purification of cytochrome P-450 from rat lung microsomes" @default.
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- W2068124326 doi "https://doi.org/10.1016/0006-291x(75)90120-5" @default.
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