硫氧还蛋白或谷胱甘肽对小鼠包皮腺雄激素受体的再激活作用。

Reactivation of the androgen receptor from murine preputial gland by thioredoxin or GSH.

作者信息

Wiegand M, Ofenloch-Hähnle B, Eisele K

机构信息

Physiologisch-Chemisches Institut, Universität, Tübingen, F.R.G.

出版信息

J Steroid Biochem. 1989 Jan;32(1A):53-8. doi: 10.1016/0022-4731(89)90013-7.

DOI:10.1016/0022-4731(89)90013-7

PMID:2913401

Abstract

The androgen receptor from murine preputial gland was inactivated by density gradient centrifugation, affinity chromatography and isoelectric focusing. The hormone binding of the receptor could be partially restored (roughly 40%) by the thioredoxin-thioredoxinreductase system, by thioredoxin plus dithiothreitol or by glutathione. Dithiothreitol, by itself, was unable to reactivate the androgen receptor. These findings show that the receptor inactivation is, at least partially, due to thiol group oxidation and removal of SH-reducing and/or -stabilizing substances from the receptor during purification.

摘要

来自小鼠包皮腺的雄激素受体通过密度梯度离心、亲和层析和等电聚焦使其失活。该受体的激素结合能力可通过硫氧还蛋白-硫氧还蛋白还原酶系统、硫氧还蛋白加二硫苏糖醇或谷胱甘肽部分恢复（约40%）。二硫苏糖醇自身无法使雄激素受体重新激活。这些发现表明，受体失活至少部分是由于在纯化过程中硫醇基团氧化以及从受体中去除了SH-还原和/或 -稳定物质。