Physicochemical characterization of the androgen receptor in rat uterine cytosol.
In this manuscript a number of physicochemical and DNA-binding properties of the androgen receptor from rat uterus were characterized. The dissociation of [3H]testosterone from the receptor followed first order kinetics, with a half-time dissociation rate of approximately 48 h at 0 C. Maximum binding was maintained at pH 7. Ammonium sulfate precipitated the receptor at concentrations between 25-40% saturation. Gel filtration and sucrose gradient analysis revealed a 62 A, 6S binding component (mol wt, 167,000; frictional ratio, 1.71) in both the absence and presence of the protease inhibitor leupeptin. Isoelectric focusing revealed an isoelectric point of 5.9. The receptor bound to DEAE-agarose, heparin-Sepharose, and hydroxylapatite. Increased receptor binding to phosphocellulose and DNA-cellulose was observed after heat treatment at 24 C for 30 min. These results demonstrate that the uterine androgen receptor has many properties similar to those of androgen receptors in male target tissues.
D000645:Ammonium Sulfate; D000818:Animals; D002482:Cellulose / Q000031:analogs & derivatives / Q000378:metabolism; D055598:Chemical Phenomena; D011232:Chemical Precipitation; D002627:Chemistry, Physical; D003600:Cytosol / Q000378:metabolism*; D004247:DNA / Q000378:metabolism; D005260:Female; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D007700:Kinetics; D051381:Rats; D011919:Rats, Inbred Strains; D011944:Receptors, Androgen / Q000378:metabolism*; D011987:Receptors, Steroid / Q000378:metabolism*; D013739:Testosterone / Q000378:metabolism; D014599:Uterus / Q000378:metabolism*
D011944:Receptors, Androgen; D011987:Receptors, Steroid; D013739:Testosterone; D002482:Cellulose; D004247:DNA; C008881:phosphocellulose; D000645:Ammonium Sulfate