Smirnov A N, Smirnova O V, Fisher U M, Rozen B V
Biull Eksp Biol Med. 1976 Jan;81(1):68-70.
Some properties of the macromolecules of the KCl-extracts of the nuclei of the uterus, kidney, liver, testis and prostate, specifically binding estradiol (E2), were studied. These macromolecules of the uterus and the liver were found to be maximally extracted from chromatin by the 0.6 M KCl concentration. The capacity of the macromolecules of the uterine, kidney and liver nuclear extracts to bind E2 specifically is destroyed completely by pronase, but not by RNA-ASe and DNA-ase, pointing to the protein nature of these macromolecules. Only estrogenic compounds, but not testosterone, 5alpha-dihydrotestosterone, progesterone or corticosterone were capable to compete with H3--E2 for the E2--binding sites of the macromolecules of the nuclear extracts of all the organs investigaeted. It is assumed that macromolecules of the nuclei of the investigated nontarget organs specifically binding E2 are estrogen receptors.
对子宫、肾脏、肝脏、睾丸和前列腺细胞核的KCl提取物中能特异性结合雌二醇（E2）的大分子的一些特性进行了研究。发现子宫和肝脏的这些大分子在0.6M KCl浓度下从染色质中提取量最大。子宫、肾脏和肝脏核提取物中大分子特异性结合E2的能力被链霉蛋白酶完全破坏，但不被RNA酶和DNA酶破坏，这表明这些大分子具有蛋白质性质。在所研究的所有器官的核提取物中，只有雌激素化合物，而不是睾酮、5α-二氢睾酮、孕酮或皮质酮，能够与H3-E2竞争大分子的E2结合位点。据推测，所研究的非靶器官细胞核中特异性结合E2的大分子是雌激素受体。
