Asselin J, Labrie F, Kelly P A, Philibert D, Raynaud J P
Steroids. 1976 Mar;27(3):395-404. doi: 10.1016/0039-128x(76)90059-3.
Properties of a progesterone receptor present in the cytosol (105,000 xg supernatant) of dimethylbenzanthracene (DMBA)-induced mammary tumors were studied using the highly potent progestin [3H]R 5020 (17, 21-dimethyl-19-nor-pregna-4, 9-diene-3,20-dione). As shown by sucrose gradient analysis, specific binding of [3H] R 5020 is associated with components migrating at 7-8S and 4S. Low affinity binding of the synthetic progestin is eliminated by treatment with dextran-coated charcoal. [3H] R 5020 binding is highly progestin-specific since it is easily displaced by unlabelled norgestrel, R 5020 and progesterone while estradiol-17beta, dihydrotestosterone, testosterone, testosterone and diethylstilbestrol have much lower activity. Dexamethasone and cortisol have little, if any, effect on [3H] R 5020 binding.
使用高效孕激素[3H]R 5020（17,21-二甲基-19-去甲孕-4,9-二烯-3,20-二酮）研究了二甲基苯并蒽（DMBA）诱导的乳腺肿瘤细胞溶质（105,000 xg上清液）中存在的孕激素受体的特性。蔗糖梯度分析表明，[3H]R 5020的特异性结合与迁移率为7-8S和4S的组分相关。合成孕激素的低亲和力结合可通过用葡聚糖包被的活性炭处理来消除。[3H]R 5020结合具有高度的孕激素特异性，因为它很容易被未标记的炔诺酮、R 5020和孕酮取代，而雌二醇-17β、双氢睾酮、睾酮和己烯雌酚的活性则低得多。地塞米松和皮质醇对[3H]R 5020结合几乎没有影响。
