Cytochrome P-450 Purified to Apparent Homogeneity from Fhenoba~ital-induced Rabbit Liver Mi~roso~s: ~at~yti~ Activity and Other Properties*
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چکیده
Cytochrome P-450 was purified to a content of over 17 nmoles Sunmarc per mg of protein from liver microsomes of phenobarbital-treated rabbits by fractionation with polyethylene glycol 6000, DEAE-cellulose colunn chromatography, and hydroxylapatite column chromatography in the presence of Renex 690, a nonionic detergent. The purified preparation exhibited a single polypeptide band (molecular weight, 49,000 daltons) when submitted to SDS-polyacrylamide gel electrophoresis. chrome 2 reductase were absent. Cytochromes P-420 and & and NADPH-cytoThe reconstituted system containing purified cytochrome P-450, reductase, and phosphatidylcholine catalyzed the hydroxylation of benzphetamine, cyclohexane, aniline, and laurate.
منابع مشابه
Purification and properties of P-450LM3b, a constitutive form of cytochrome P-450, from rabbit liver microsomes.
This laboratory has previously reported the occurrence in rabbit liver microsomes of a non-inducible form of cytochrome P-450, designated P-45Dwsb because of its electrophoretic mobility relative to that of phenobarbital-inducible P-45Owz and 5,6-benzoflavone-inducible P-450~~~. In the present study, P'45Dmsb was purified to electrophoretic homogeneity and a specific content of over 19 nmol per...
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