Abstract
A 5α-dihydrotestosterone binding component, sedimenting with a sedimentation constant of 8.6S, was detected in rat hypothalamic cytosol labelled in vitro with 5α-dihydrotestosterone-3H. The dissociation constant of the androgen-protein complex and the number of binding sites of the component were approximately 7.4×10-10M and 0.9×10-14 moles/mg cytosol protein, respectively. The binding component seemed to have a specificity for 5α-dihydrotestosterone relative to other hormones. These results suggest that the cytosol from male rat hypothalamus contains “receptor” for 5α-dihydrotestosterone.
