Purification of the steroid-binding core of porcine estrogen receptor.
The steroid-binding core of estradiol receptor was purified from pig uterus cytosol by a protocol consisting of (1) adsorption to heparin-sepharose, (2) enzymatic release of the receptor core, (3) DEAE-chromatography, (4) Sephadex G-150 filtration and (5) chromatography on heparin-sepharose. The final product was approximately 18000-fold enriched over the starting material. It consisted of at least 18% core protein resembling dimeric microsomal receptor with a molecular mass of 75 kDa and an isoelectric point of 5.8 (microheterogeneity). A goat antiserum raised against the preparation contains immunoglobulins G precipitating estradiol-receptor complexes, and antibodies releasing the steroid from its binding site.
D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D003600:Cytosol / Q000032:analysis; D004958:Estradiol / Q000378:metabolism; D005260:Female; D006041:Goats / Q000276:immunology; D007525:Isoelectric Focusing; D008861:Microsomes / Q000378:metabolism; D011960:Receptors, Estrogen / Q000302:isolation & purification*; D013552:Swine; D014599:Uterus / Q000378:metabolism
D011960:Receptors, Estrogen; D004958:Estradiol