A DEHYDROEPIANDROSTERONE SULFATASE INHIBITORY ACTIVITY IN SOLUBLE-PROTEINS OF GUINEA-PIG LIVER

被引：5

作者：

MOUTAOUAKKIL, M ^{[1
]}

ADESSI, GL ^{[1
]}

机构：

[1] INSERM, U198, UNITE RECH BIOCHIM HORMONALE & REGULAT, ROUTE DOLE, F-25000 BESANCON, FRANCE

来源：

STEROIDS | 1986年 / 47卷 / 06期

关键词：

D O I：

10.1016/0039-128X(86)90055-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

An inhibitor of microsomal dehydroepiandrosterone sulfatase was found in the soluble fraction of non-pregnant guinea pig liver. The extent of inhibitory effect was dependent on the concentration of soluble proteins. The inhibitor was partly purified by gel permeation and hydroxylapatite chromatography with a purification factor of 16.6. The soluble inhibitor was non-dialyzable, not destroyed by RNase or DNase digestion but totally destroyed by pronase digestion. The inhibitor is a soluble protein with a molecular weight of approximately 17,000 (determined by gel permeation chromatography). Inhibition of microsomal dehydroepiandrosterone sulfatase by the soluble inhibitor is a non-competitive inhibition. From this present finding the question arises whether the inhibitor could be involved in the regulation of the hydrolysis of dehydroepiandrosterone sulfate in the guinea pig liver.

引用

页码：401 / 411

页数：11

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