Gyorki S, James R, Warne G L, Funder J W
J Steroid Biochem. 1986 Sep;25(3):355-8. doi: 10.1016/0022-4731(86)90247-5.
Androgen receptors were partially purified by affinity chromatography of cytosols prepared from either normal foreskins or normal cultured fibroblasts. Partially purified receptors were covalently labelled with [3H]R1881 (tritiated methyltrienolone) by ultraviolet photoactivation. Gel electrophoresis of cytosols from both sources showed two peaks of specific binding, Mr approximately 40 K and approximately 85 K, under denaturing conditions. Photoaffinity labelling of the human androgen receptor may thus provide a useful tool in further studies on disorders of androgenization.
通过对从正常包皮或正常培养的成纤维细胞制备的胞质溶胶进行亲和层析，部分纯化雄激素受体。通过紫外线光激活，将部分纯化的受体与[3H]R1881（氚化甲基三烯醇酮）共价标记。在变性条件下，来自这两种来源的胞质溶胶的凝胶电泳显示出两个特异性结合峰，分子量分别约为40K和约85K。因此，人雄激素受体的光亲和标记可能为进一步研究雄激素化障碍提供有用的工具。
