Androgen binding in the baboon prostate.

J P Karr; R Y Kirdani; G P Murphy; A A Sandberg

doi:10.3109/01485017908987303

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Androgen binding in the baboon prostate.

J P Karr·R Y Kirdani·G P Murphy·A A Sandberg

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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.

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Animals Binding, Competitive Cyproterone Dihydrotestosterone Haplorhini Male Papio Prostate Receptors, Androgen Receptors, Steroid Sex Hormone-Binding Globulin Journal Article Research Support, U.S. Gov't, P.H.S.

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J P Karr, R Y Kirdani, G P Murphy, A A Sandberg. 1979. Androgen binding in the baboon prostate.. https://doi.org/10.3109/01485017908987303

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