IDENTIFICATION OF THE HUMAN LIVER CYTOCHROME-P-450 RESPONSIBLE FOR COUMARIN 7-HYDROXYLASE ACTIVITY

被引：201

作者：

MILES, JS ^{[1
]}

MCLAREN, AW ^{[1
]}

FORRESTER, LM ^{[1
]}

GLANCEY, MJ ^{[1
]}

LANG, MA ^{[1
]}

WOLF, CR ^{[1
]}

机构：

[1] UNIV KUOPIO,DEPT PHARMACOL & TOXICOL,SF-70211 KUOPIO 21,FINLAND

来源：

BIOCHEMICAL JOURNAL | 1990年 / 267卷 / 02期

关键词：

D O I：

10.1042/bj2670365

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：

1. We have constructed a full-length human liver cytochrome P450IIA cDNA from a partial-length clone by oligonucleotide-directed mutagenesis, and subcloned it into the monkey kidney (COS-7) cell expression vector, pSVL. 2. The cDNA encodes a 49 kDa protein with coumarin 7-hydroxylase (COH) activity which cross-reacts with antisera to the mouse cytochrome P-450 isoenzyme responsible for COH activity and comigrates with a human liver microsomal protein. 3. Western blot analysis of a panel of human livers indicates that the level of the 40 kDa protein, detected using antisera to either the mouse COH P-450 or rat P450IIA1 protein, correlates very highly with COH activity. 4. Antisera to the rat P450IIA1 protein can inhibit COH activity in human liver microsomes. Taken together, these data indicate that a member of the P450IIA subfamily is responsible for most, if not all, of the COH activity in human liver.

引用

页码：365 / 371

页数：7

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