PARTIAL-PURIFICATION OF HUMAN-LIVER CYTOCHROME-P-450

被引：52

作者：

BEAUNE, P ^{[1
]}

DANSETTE, P ^{[1
]}

FLINOIS, JP ^{[1
]}

COLUMELLI, S ^{[1
]}

MANSUY, D ^{[1
]}

LEROUX, JP ^{[1
]}

机构：

[1] ECOLE NORM SUPER,CNRS,CHIM LAB 32,F-75231 PARIS 5,FRANCE

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 88卷 / 03期

关键词：

D O I：

10.1016/0006-291X(79)91482-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Human liver cytochrome P 450 was partially purified by hydrophobic chromatography on Octyl-Sepharose, followed by ion-exchange chromatography on DEAE-cellulose. Two fractions (A and B) were obtained; cytochrome P 450 of fraction A was purified sixfold, with an overall yield of about 6 %. Its spectral properties were similar to those previously described in animal cytochromes P 450. Moreover, p-nitroanisole-O-demethylase activity could be obtained in a reconstituted system involving cytochrome P 450 of fraction A, human NADPH-cytochrome c reductase and phospholipids. © 1979.

引用

页码：826 / 832

页数：7

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