Barrack E R
Endocrinology. 1983 Jul;113(1):430-2. doi: 10.1210/endo-113-1-430.
In cell-free binding experiments, androgen receptors of rat ventral prostate cytosol bound with high affinity (Kd = 10(-10) M) to a saturable number of sites (acceptors) associated with the nuclear matrix of the prostate. This binding was dependent on the presence of an activated androgen-receptor complex. In addition, the binding was tissue-specific, since liver nuclear matrix, in contrast, contained only 15-20% as many acceptors for androgen receptors as the prostate nuclear matrix. The prostate nuclear matrix contained approximately 75% of the number of total nuclear acceptor sites. Matrix-associated acceptor sites appear to be associated with the internal RNA-protein network of the nuclear matrix since the peripheral lamina component of the matrix bound only 30% as many receptors as the intact nuclear matrix.
在无细胞结合实验中,大鼠腹侧前列腺胞质溶胶中的雄激素受体以高亲和力(Kd = 10⁻¹⁰ M)与前列腺核基质相关的可饱和数量的位点(受体)结合。这种结合依赖于活化的雄激素 - 受体复合物的存在。此外,这种结合具有组织特异性,因为相比之下,肝核基质所含的雄激素受体受体位点数量仅为前列腺核基质的15 - 20%。前列腺核基质包含大约75%的总核受体位点数量。与基质相关的受体位点似乎与核基质的内部RNA - 蛋白质网络相关,因为基质的外周板层成分结合的受体数量仅为完整核基质的30%。