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Endocrinology, Vol 98, 1206-1213, Copyright © 1976 by Endocrine Society
ARTICLES |
JR Schreiber, R Reid and GT Ross
A soluble thermolabile protein with many characteristics of an androgen receptor has been demonstrated for the first time in the cytosol (100,000 X g supernatant) of estrogen-stimulated ovaries from hypophysectomized immature female rats (HIFR) treated with diethylstilbestrol in Silastic capsules (DESC). This binding protein is organ-specific and androgen-specific, has a high affinity with a Kd of 2.4 X 10(-9)M for testosterone, and is saturable with 2.1 X 10(-13) moles of binding sites per mg cytosol protein. The number of binding sites is linear with cytosol protein concentration and the binding protein sediments at 7-8 S on sucrose gradients. Estradiol is an effective inhibitor of testosterone binding. A role for this testosterone-binding protein as an effector of ovarian morphologic change is hypothesized.
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