Identification of a high affinity nuclear acceptor site for estrogen receptor of calf uterus.
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.
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002467:Cell Nucleus / Q000378:metabolism; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004247:DNA; D003851:Deoxyribonucleases / Q000378:metabolism; D004958:Estradiol / Q000378:metabolism*; D005260:Female; D006882:Hydroxyapatites; D009698:Nucleoproteins / Q000302:isolation & purification* / Q000378:metabolism; D011134:Polysaccharides; D011402:Pronase / Q000378:metabolism; D011956:Receptors, Cell Surface; D012260:Ribonucleases / Q000378:metabolism; D014316:Tritium; D014357:Trypsin / Q000378:metabolism; D014599:Uterus / Q000166:cytology / Q000378:metabolism*
D006882:Hydroxyapatites; D009698:Nucleoproteins; D011134:Polysaccharides; D011956:Receptors, Cell Surface; D014316:Tritium; D004958:Estradiol; D004247:DNA; D003851:Deoxyribonucleases; D012260:Ribonucleases; D014357:Trypsin; D011402:Pronase