A gel-electrophoretically homogeneous preparation of cytochrome P-450 from liver microsomes of phenobarbital-pretreated rabbits |
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Authors: | Y Imai R Sato |
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Institution: | Institute for Protein Research, Osaka University, Suita, Osaka 565, Japan |
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Abstract: | Cytochrome P-450 was purified from liver microsomes of phenobarbital-pretreated rabbits to a specific content of 16 to 17 nmoles per mg of protein with a yield of about 10 %. The purified cytochrome yielded only a single protein band on sodium dodecylsulfate-urea-polyacrylamide gel electrophoresis, and an apparent molecular weight of about 45,000 was estimated for the protein. The preparation was free of cytochrome , NADH-cytochrome reductase, and NADPH-cytochrome reductase activities. Aniline hydroxylase and ethylmorphine N-demethylase activities could be reconstituted upon mixing the purified cytochrome with an NADPH-cytochrome reductase preparation (purified by a detergent method) and phosphatidyl choline. |
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Keywords: | PB phenobarbital SDS sodium dodecylsulfate |
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