The presence of a cytoplasmic estrogen receptor in sexually mature rabbit epididymides: comparison with the estrogen receptor in immature rabbit epididymal cytosol.

Cytosol prepared from epididymides of castrated adult rabbits contains an estrogen-specific binding component that sediments in the 4--5S region on 0.01 M KCl sucrose gradients. The estrogen-specific binding component is not detectable on sucrose gradients unless the cytosol-[3H]estradiol mixture is first extracted with charcoal to remove uncomplexed and rapidly exchangeable ligand from the sample. The macromolecular bound [3H]estradiol that remains after charcoal extraction dissociates from the receptor with a dissociation half-time of greater than 24 h and is of high affinity (Kd = 6.5 +/- 0.9 X 10(-9) M). The estrogen receptor in the adult rabbit epididymis can also be demonstrated when charcoal-extracted samples are chromatographed on Sephadex G-200. Using this system, the major estrogen-specific binder has an apparent molecular weight of less than 200,000. In contrast, the epididymal estrogen receptor in sexually immature rabbits sediments as an 8S species on low salt gradients and has an apparent molecular weight of 200,000 or greater when assessed by chromatography on Sephadex G-200. The estrogen receptor in both age groups is distributed along the length of the epididymal duct. The highest concentration of the cytoplasmic receptor in both mature and immature rabbits is in the cauda epididymidis. The age-dependent changes in the amount of the receptor suggest that it may be involved in maturational changes in the epididymis. The alterations in the physicochemical properties may reflect physiological changes in the epididymis or in the endocrine status of the animal.