Abstract

The cytosol 17β-estradiol receptors from rabbit kidney, liver and uterus, compared under identical experimental conditions, were similar in terms of their pH-activity profiles, dependence on incubation temperature, sensitivity to sulfhydryl reagents and steroid specificity. 17β-[ 3H]-Estradiol binding was saturable with all three tissues, having an apparent dissociation constant of 4 × 10 −10 M. The binding of 17β-[ 3H]-estradiol in kidney, liver and uterus was inhibited by estrogens, including estrogen conjugates, but not by testosterone, progesterone or cortisol. The 17β-estradiol receptors of liver, kidney and uterus exhibited significant differences with respect to their Chromatographie behaviour on heparinSepharose. Furthermore, a comparison of their sucrose density gradient centrifugation patterns showed that the 17β-[ 3H]-estradiol-receptor complex of liver and kidney sedimented at 3-4 S in both low and high ionic strength media, while the uterine receptor sedimented at 7–8 S in low ionic strength media and at 4–5 S in high ionic strength media. When the liver and uterine cytosol fractions were combined the uterine receptor was altered and sedimented at 3–4 S in low ionic strength media.

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