Androgen receptor in genital tubercle of rabbit fetuses and newborns. Ontogeny and properties.
In newborn rabbits of both sexes, an androgen receptor was characterized in the genital tubercle. Homogenates exhibited high affinity (Kd was about 0.4 nM) and saturable binding of [3H]methyltrienolone. The half-life of the [3H]5 alpha-dihydrotestosterone-androgen receptor complex was 72 h at 4 degrees C. The receptor was inactivated by heat and pronase and the binding was specific for potent androgens. Sucrose gradient analysis revealed a 8-9 S [3H]methyltrienolone binding protein in cytosols from both sexes. Androgen binding, in the homogenate, was detected as soon as day 18 of gestation in both sexes and the number of binding sites increased until birth. During sexual organogenesis and at birth there were no major differences between males and females in the amount or affinity of androgen binding. Specific androgen binding was also detected in sexual ducts of male and female newborns.
D000818:Animals; D000831:Animals, Newborn / Q000378:metabolism; D002499:Centrifugation, Density Gradient; D005260:Female; D005333:Fetus / Q000032:analysis*; D005836:Genitalia, Female / Q000032:analysis* / Q000196:embryology; D005837:Genitalia, Male / Q000032:analysis* / Q000196:embryology; D006358:Hot Temperature; D066298:In Vitro Techniques; D008297:Male; D011247:Pregnancy; D011402:Pronase / Q000494:pharmacology; D011817:Rabbits; D011944:Receptors, Androgen / Q000032:analysis*; D012733:Sex Differentiation; D012737:Sex Factors; D014316:Tritium
D011944:Receptors, Androgen; D014316:Tritium; D011402:Pronase