Purification of a substrate complex of cytochrome P-450 from liver microsomes of 3-methylcholanthrene-treated rabbits. |
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Authors: | C Hashimoto Y Imai |
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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 as a 3-methylcholanthrene complex from liver microsomes of 3-methylcholanthrene-treated rabbits to a specific content of 17 to 18 nmoles per mg of protein with a yield of about 10 %. The purified protein gave only a single protein band on sodium dodecylsulfate-urea-poly-acrylamide gel electrophoresis, and its apparent molecular weight was estimated to be about 54,000, a value which is higher than that for cytochrome P-450 from phenobarbital-treated rabbits by about 4,000. The reconstituted system containing the purified cytochrome and NADPH-cytochrome reductase was active in NADPH-dependent hydroxylation of benzoα]pyrene. |
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Keywords: | PB phenobarbital MC 3-methylcholanthrene DTT dithiothreitol |
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