Identification and partial characterization of the cytoplasmic androgen receptor in bovine ovarian capsule.
[3H]Dihydrotestosterone (DHT) binding to a specific protein in the cytosol of bovine ovarian capsule was studied in vitro. The specific androgen-binding protein in the cytosol was analyzed by chromatographic and ultracentrifugal techniques. From Scatchard analysis, the dissociation constant was 7.4 nM and the number of binding sites was 58.8 fmol/mg protein. Testosterone and 17 alpha-methyltrienolone (R1881) compete for [3H]DHT binding. In the presence of sodium molybdate and at low salt concentrations, the steroid-protein complex sediments as a 9S form, while in the presence of high salt, it sediments at 3.5S. In the absence of molybdate or in the presence of high salt, the 9S form dissociates in a temperature-dependent manner into smaller units. These properties are consistent with the presence of a typical androgen receptor in the bovine ovarian capsule.
D000818:Animals; D001667:Binding, Competitive; D002417:Cattle; D002499:Centrifugation, Density Gradient; D002850:Chromatography, Gel; D003593:Cytoplasm / Q000378:metabolism; D013196:Dihydrotestosterone / Q000378:metabolism; D004963:Estrenes / Q000378:metabolism; D005260:Female; D006358:Hot Temperature; D015741:Metribolone; D008982:Molybdenum / Q000494:pharmacology; D009994:Osmolar Concentration; D010053:Ovary / Q000378:metabolism*; D011944:Receptors, Androgen / Q000378:metabolism*; D011987:Receptors, Steroid / Q000378:metabolism*; D013739:Testosterone / Q000378:metabolism
D004963:Estrenes; D011944:Receptors, Androgen; D011987:Receptors, Steroid; D013196:Dihydrotestosterone; D015741:Metribolone; D013739:Testosterone; D008982:Molybdenum; C024687:sodium molybdate(VI)