期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1974
卷号：71
期号：3
页码：979-983
DOI：10.1073/pnas.71.3.979
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：By means of affinity chromatography, specific nuclear acceptor sites for estradiol receptors are identified in a fraction that can be solubilized from purified nuclei with 2 M NaCl. Interaction between these acceptor sites and crude or partially purified estradiol receptor shows a high association constant (over 109 M). Receptor-acceptor interaction is dependent on physiological concentrations of 17{beta}-estradiol; it is disrupted by high ionic strength. The nuclear acceptor sites appear to be protein in nature and exist in 5- to 10-fold excess over the estrogen binding sites present in the cytosol. Single- or double-stranded DNA does not bind estrogen-receptor complexes. Acceptor sites appear to be associated with basic nuclear proteins as judged by hydroxyapatite chromatography. The nuclear acceptor sites probably represent less than 0.1% of the purified basic proteins from the nucleus.
关键词：affinity chromatography ; basic proteins ; DNA
