Differential release of estradiol from immobilized estrogen receptors by p-sec-amylphenol: evidence for a functional microheterogeneity of estrogen receptors.
3H-Estradiol-estrogen receptor complexes were adsorbed on a column of heparin-agarose and subjected to a gradient of increasing concentrations of p-sec-amylphenol. At least five peaks of released 3H-estradiol were observed--demonstrating the existence of subsets of heparin-immobilized receptors with different affinities for estradiol. This finding is presented as further evidence for a functional micro-heterogeneity among estrogen receptors. The origin of the observed differences in estrogen receptors and possible relevance of the findings to receptor-mediated responses are discussed.
D000818:Animals; D003600:Cytosol / Q000378:metabolism; D004958:Estradiol / Q000378:metabolism*; D005260:Female; D066298:In Vitro Techniques; D010636:Phenols / Q000494:pharmacology*; D011817:Rabbits; D051381:Rats; D011960:Receptors, Estrogen / Q000187:drug effects* / Q000378:metabolism; D012685:Sepharose / Q000031:analogs & derivatives; D014599:Uterus / Q000378:metabolism
D010636:Phenols; D011960:Receptors, Estrogen; C037405:heparin-sepharose; C018828:p-sec-amylphenol; D004958:Estradiol; D012685:Sepharose