Abstract
A cell-free system prepared from the ovariectomized rat uterus was used to study the uptake of the cytoplasmic estrogen receptor (RE) by isolated nuclei. At 0–4 C, dialysis of cytosol containing [3H]estradiol (E2)-RE complexes resulted in a 3- to 6-fold increase in nuclear binding of [3H]E2-RE in comparison with nondialyzed cytosol. Removal of the low molecular weight materials by Sephadex G-25 chromatography also enhanced binding of [3H]E22-RE complexes to nuclei. Incubation of nuclei at 0 C with cytosol dialyzed in the absence of estrogen revealed the appearance of the estrogen-binding component in nuclei which showed high affinity for EE (Kd = 6 × 10-10 M at 0 C). This nuclear estrogen-binding component was not occupied with estrogen, since a slightly higher amount of binding with [3H]EE was obtained at 0 than at 37 C. The effects of dialysis on the sedimentation constants were also studied. Dialysis of [3H]E2-RE complexes in cytosol at 0–4 C caused a change of the sedimentation constant from 4.3S to 5...
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