豚鼠肝脏可溶性蛋白中的硫酸脱氢表雄酮硫酸酯酶抑制活性。

A dehydroepiandrosterone sulfatase inhibitory activity in soluble proteins of guinea pig liver.

作者信息

Moutaouakkil M, Adessi G L

出版信息

Steroids. 1986 Jun;47(6):401-11. doi: 10.1016/0039-128x(86)90055-3.

Abstract

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.

摘要

在未孕豚鼠肝脏的可溶部分发现了一种微粒体脱氢表雄酮硫酸酯酶抑制剂。抑制作用的程度取决于可溶蛋白的浓度。通过凝胶渗透和羟基磷灰石色谱法对该抑制剂进行了部分纯化，纯化因子为16.6。可溶性抑制剂不可透析，不受核糖核酸酶或脱氧核糖核酸酶消化的破坏，但可被链霉蛋白酶消化完全破坏。该抑制剂是一种可溶性蛋白质，分子量约为17,000（通过凝胶渗透色谱法测定）。可溶性抑制剂对微粒体脱氢表雄酮硫酸酯酶的抑制作用是非竞争性抑制。根据目前的这一发现，产生了一个问题，即该抑制剂是否可能参与豚鼠肝脏中脱氢表雄酮硫酸酯水解的调节。