Aubry M, Collu R, Ducharme J R, Crine P
Endocrinology. 1982 Dec;111(6):2129-31. doi: 10.1210/endo-111-6-2129.
The Leydig cells of the testis are known to possess high affinity receptors for luteinizing hormone and human chorionic gonadotropin (hCG), but no information concerning the synthesis of these receptors is available yet. In order to investigate this question, we have purified crude rat interstitial cell preparations on discontinuous Percoll gradients, and Leydig cells recovered from fractions demonstrating maximum testosterone production and hCG binding capacity were incubated for 17 h in a culture medium containing [35S]methionine. Radioactive proteins solubilized with Triton X-100 were submitted to affinity chromatography on a resin consisting of hCG covalently linked to agarose. Proteins bound to the column were analyzed by two-dimensional gel electrophoresis. Autoradiography of the gel revealed a major protein (molecular weight: 79,000; pI 4.5) whose binding to the resin could be greatly diminished by an excess of hCG. The electrophoretic properties of this protein are similar to those of previously isolated gonadotropin receptor components.
已知睾丸的间质细胞对促黄体生成素和人绒毛膜促性腺激素（hCG）具有高亲和力受体，但关于这些受体的合成尚无相关信息。为了研究这个问题，我们在不连续的Percoll梯度上纯化了大鼠间质细胞粗提物，并将从显示最大睾酮生成和hCG结合能力的组分中回收的间质细胞在含有[35S]甲硫氨酸的培养基中孵育17小时。用Triton X-100溶解的放射性蛋白质在由与琼脂糖共价连接的hCG组成的树脂上进行亲和层析。通过二维凝胶电泳分析与柱结合的蛋白质。凝胶的放射自显影显示一种主要蛋白质（分子量：79,000；等电点4.5），过量的hCG可大大减少其与树脂的结合。该蛋白质的电泳性质与先前分离的促性腺激素受体组分相似。
