Ross P, Ruh T S
Biochim Biophys Acta. 1984 May 15;782(1):18-25. doi: 10.1016/0167-4781(84)90101-5.
Non-histone protein-DNA complexes with acceptor activity for estradiol-receptor complexes were reconstituted from fractionated calf uterine chromatin. Acceptor activity had tissue specificity with target tissue binding exceeding non-target tissue binding. The binding of estradiol-receptor complexes to acceptor sites was dependent on intact non-histone protein-DNA complexes, reconstituted select non-histone proteins, and protein equivalent: DNA reconstitution ratios. [3H]Estradiol-receptor complexes were bound to reconstituted non-histone protein-DNA complexes (i.e., nucleoacidic protein) with a high affinity and with a limited number of binding sites. Fractionation of uterine chromatin non-histone proteins identified two major sets of non-histone proteins which had acceptor activity when reconstituted with DNA. Thus, it seems possible to reconstitute nucleoacidic protein fractions with specific acceptor activity for the calf uterine estrogen receptor.
从分级分离的小牛子宫染色质中重构了对雌二醇受体复合物具有受体活性的非组蛋白 - DNA复合物。受体活性具有组织特异性，靶组织结合超过非靶组织结合。雌二醇受体复合物与受体位点的结合取决于完整的非组蛋白 - DNA复合物、重构的特定非组蛋白以及蛋白质当量与DNA重构比率。[3H]雌二醇受体复合物以高亲和力且结合位点数量有限地结合到重构的非组蛋白 - DNA复合物（即核酸蛋白）上。子宫染色质非组蛋白的分级分离鉴定出两组主要的非组蛋白，当与DNA重构时具有受体活性。因此，似乎有可能重构对小牛子宫雌激素受体具有特异性受体活性的核酸蛋白组分。
