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Isolation and partial characterization of a rifampicin induced rabbit liver microsomal cytochrome P-450.

作者信息

Lange R, Larroque C, Balny C, Maurel P

出版信息

Biochem Biophys Res Commun. 1985 Jan 31;126(2):833-9. doi: 10.1016/0006-291x(85)90260-8.

DOI:10.1016/0006-291x(85)90260-8
PMID:3919717
Abstract

Rifampicin administration to New Zealand male rabbits increased the concentration of an LM3 form of cytochrome P-450 to up to 30% of the microsomal P-450 concentration. This enzyme was purified to electrophoretic homogeneity with a yield of 8% of the original total microsomal P-450 concentration. Isolated as a low spin hemoprotein in its substrate free oxidized form, it displays in its reduced CO-complexed form an absorption maximum at 449 nm. Immunological assays, as well as activity measurements, in particular its stereospecific progesterone hydroxylation in the 6 beta-position, show a relationship between LM3,Rif and LM3c (from untreated rabbits).

摘要

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Cloning of a cDNA coding for P-450 LM3c from rabbit liver microsomes and regulation of its expression.从兔肝微粒体中克隆编码P-450 LM3c的cDNA及其表达调控
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