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循环系统中的皮质类固醇侧链异构酶。

Corticosteroid side-chain isomerase in the circulatory system.

作者信息

Monder C, Marandici A

机构信息

Population Council, New York, NY 10021.

出版信息

Steroids. 1991 Jan;56(1):12-6. doi: 10.1016/0039-128x(91)90108-8.

Abstract

Corticosteroid side-chain (CSC) isomerase catalyzes ketol-aldol interconversion of the corticosteroid side chain. The enzyme was present in the blood of mouse, rat, guinea pig, chicken, pig, horse, sheep, cow, and human. The patterns of substrate specificity, measuring 3H-1H exchange of 21-tritiated forms of 11-deoxycorticosterone, corticosterone, and cortisol, were species specific. Based on enzyme activity and immunostaining of mouse blood fractions, red blood cells had the most isomerase activity, plasma had less, and white blood cells had low but highly variable levels of enzyme. Purified mouse liver CSC isomerase was found to be adsorbed by red blood cells. The results suggest that circulating CSC isomerase is derived in part from tissue sources and is in part an intrinsic blood enzyme.

摘要

皮质类固醇侧链(CSC)异构酶催化皮质类固醇侧链的酮醇-醛醇互变。该酶存在于小鼠、大鼠、豚鼠、鸡、猪、马、羊、牛和人的血液中。以11-脱氧皮质酮、皮质酮和皮质醇的21-氚代形式的3H-1H交换来衡量的底物特异性模式具有物种特异性。根据小鼠血液组分的酶活性和免疫染色,红细胞具有最高的异构酶活性,血浆中的活性较低,白细胞的酶活性低但水平变化很大。发现纯化的小鼠肝脏CSC异构酶可被红细胞吸附。结果表明,循环中的CSC异构酶部分来源于组织,部分是一种内在的血液酶。

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