Identification of a High Affinity Nuclear Acceptor Site for Estrogen Receptor of Calf Uterus
- 1 March 1974
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 71 (3) , 979-983
- https://doi.org/10.1073/pnas.71.3.979
Abstract
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 10(9) M). Receptor-acceptor interaction is dependent on physiological concentrations of 17beta-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.Keywords
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