Smirnova O V, Smirnov A N, Khodakova T K, Rozen V B
Probl Endokrinol (Mosk). 1975 May-Jun;21(3):71-6.
A study was made of specific binding of estradiol (E2) by cytosol and the extracts of the nuclei of the testes, the prostate, the kidneys and the liver of the sexually-mature male rats. In the cytosol of all the mentioned organs there were found macromolecules with a high affinity (Kac similar 1--4-10(9)M(-1)). Low capacity ti the hormone (Nc similar to (1--2)--minus 14 mol per 1 mg of protein) and a marked hormonal sterospecificity--only the preparations with an estrogenic activity, but not testosterone, 5alpha-dihydrotestosterone, progesterone and corticosterone competed for H-3--E2 binding. The capacity of cytosol of these organs to bind E2 apecifically was eliminated by pronase, but not by RNA-ase and DNA-ase. The mentioned properties of the E2-binding macromolecules of cytosol of the testes, the prostate, the kidneys and the liver permitted to refer them to the estrogenic protein-receptors. Specific E2-binding was also revealed in the extracts of the nuclei of these organs, but its level was extremely low.
对性成熟雄性大鼠的睾丸、前列腺、肾脏和肝脏的胞质溶胶以及细胞核提取物中雌二醇（E2）的特异性结合进行了研究。在上述所有器官的胞质溶胶中均发现了具有高亲和力（Kac约为1 - 4×10⁹M⁻¹）的大分子。对激素的结合能力较低（Nc约为每1毫克蛋白质（1 - 2）×10⁻¹⁴摩尔），且具有显著的激素立体特异性——只有具有雌激素活性的制剂，而不是睾酮、5α - 二氢睾酮、孕酮和皮质酮，能与³H - E2结合竞争。这些器官胞质溶胶特异性结合E2的能力可被链霉蛋白酶消除，但不能被核糖核酸酶和脱氧核糖核酸酶消除。睾丸、前列腺、肾脏和肝脏胞质溶胶中E2结合大分子的上述特性使其可归为雌激素蛋白受体。在这些器官的细胞核提取物中也发现了特异性E2结合，但其水平极低。
