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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
