SUBCELLULAR-LOCALIZATION OF GUINEA-PIG HEPATIC MOLYBDENUM HYDROXYLASES

被引：22

作者：

CRITCHLEY, DJP ^{[1
]}

RANCE, DJ ^{[1
]}

BEEDHAM, C ^{[1
]}

机构：

[1] PFIZER LTD, DEPT DRUG METAB, SANDWICH CT13 9NJ, KENT, ENGLAND

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 185卷 / 01期

关键词：

D O I：

10.1016/S0006-291X(05)80954-4

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：

Molybdenum hydroxylase activity in guinea pig liver has been compared with that of marker enzymes in mitochondria(succinate dehydrogenase), microsomes (glucose-6-phosphatase) and cytosol (lactate dehydrogenase). Aldehyde oxidase activity was highest in the cytosol, with about 10-fold activity of xanthine oxidase. Significant molybdenum hydroxylase activity was found in mitochondria with minimal levels in microsomes. Mitochondrial and cytosolic aldehyde oxidase varied in substrate specificity and electrophoretic mobility with two major bands in each fraction, one of which was common to cytosol and mitochondria. © 1992 Academic Press, Inc.

引用

页码：54 / 59

页数：6

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