Receptor protein for dihydrotestosterone in nuclei of the female prostate of Praomys (Mastomys) natalensis.

An investigation was carried out to identify and characterize the binding of androgens within the nuclei of the prostate from female Praomys (Mastomys) natalensis. After in vivo and in vitro labeling with tritiated androgens, the tissue was subjected to cell fractionation and the nuclear fraction was purified. Gel exclusion chromatography and sucrose density gradient centrifugation of the nuclear extract showed the presence of a steroid receptor complex having a sedimentation coefficient of 3 S. Subsequent analysis of the bound radioactivity revealed that more than 90 per cent of the recovered tritiated steroid was dihydrotestosterone. This binding was found to be temperature dependent and could not be shown in liver tissue. The behavior of this nuclear steroid receptor complex is compared with that of the male Mastomys and the rat. It is suggested that the female Mastomys could be used as an experimental model for studying hormone effects on the prostate.