Androgen binding in the baboon prostate.
Arch Androl, 1979/3;2(2):123-6.
Karr JP, Kirdani RY, Murphy GP, Sandberg AA
PMID: 114128
Abstract
Androgen receptors were identified and partly characterized in cytosols of the caudal and cranial prostatic lobes of a 24-hr castrate baboon. Binding of cyproterone acetate (CA) to testosterone-binding globulin (TeBG) in baboon serum was negligible and therefore was an appropriate unlabeled competitor for distinguishing high-affinity binding of tritiated dihydrotestosterone (3H-DHT) to serum contaminants and receptors in cytosol preparations when multiple-point saturation analyses and removal of free steroid by charcoal adsorption were used. Specificity of androgen binding was demonstrated by the inability of diethylstilbestrol, a synthetic estrogen known to have low binding affinity for TeBG, to displace 3H-DHT from the receptor protein. The number of high-affinity binding sites and the dissociation constant of the androgen receptor calculated for the caudal lobe were 102 fmoles/mg cytosol protein and 4.0 X 10(-9) M, respectively; corresponding values for the cranial lobe were 49 fmoles and 1.3 X 10(-9) M.
MeSH terms
Animals; Binding, Competitive; Cyproterone; Dihydrotestosterone; Haplorhini; Male; Papio; Prostate; Receptors, Androgen; Receptors, Steroid; Sex Hormone-Binding Globulin
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