Action of carbon tetrachloride in the reconstituted monooxygenase system using partially purified cytochrome P-450 and P-448.

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概要

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• In the cytochrome P-450-reconstituted system, CCl<SUB>4</SUB> stimulated NADPH-dependent lipid peroxidation of the system containing the P-450 form to a much greater extent than that of the system containing the P-448 form. When the P-450-reconstituted system was preincubated in the presence of both NADPH and CCl<SUB>4</SUB>, 7-ethoxycoumarin O-deethylase, aminopyrine N-demethylase and aniline hydroxylase activities were decreased by 40-60%, whereas, with P-448 form reconstituted system, no suppression was observed in these enzyme activities or in 7-ethoxyresorufin O-deethylase activity. These observations suggest that the P-450 form, but not the P-448 form, is active in metabolizing CCl<SUB>4</SUB> to a reactive species that subsequently impairs the hemoprotein.

• 公益社団法人 日本薬理学会の論文

著者

• YASOSHIMA Mitsue

  Department of Toxicology, Niigata College of Pharmacy

関連論文

• Action of carbon tetrachloride in the reconstituted monooxygenase system using partially purified cytochrome P-450 and P-448.

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