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Chemical modification of microsomal cytochrome P450: role of lysyl residues in hydroxylation activity.

作者信息

Kunz B C, Richter C

出版信息

FEBS Lett. 1983 Sep 19;161(2):311-4. doi: 10.1016/0014-5793(83)81031-x.

DOI:10.1016/0014-5793(83)81031-x
PMID:6413255
Abstract

Cytochrome P450 purified from phenobarbital-induced rat liver microsomes was acetylated at 3 lysyl residues. When reconstituted with purified NADPH-cytochrome P450 reductase, the modified cytochrome showed full activity and substrate-induced spectral changes with d-benzphetamine. With 7-ethoxycoumarin, neither enzymic activity nor binding was detected. It is concluded that the positively charged lysine residues of cytochrome P450 are important for metabolism of 7-ethoxycoumarin by cytochrome P450.

摘要

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