Abstract
The specificity of the estrogen receptor in human uterus was determined by incubating the cytosol fraction with tritiated estradiol-17β alone or in the presence of other steroids. If the steroid competed with the estradiol-17β for binding sites on the receptor the binding of the estradiol-17β was diminished. Highest affinity to the receptor is found if the steroid has a phenolic hydroxyl group on C-3 and an alcoholic hydroxyl group on C-17 in the β-configuration. The presence of the free phenolic hydroxyl on ring A is essential and its position is of critical importance. The presence of a second oxygen function on ring D is important and its state of oxidation and its position influence the binding activity. Additional oxygen functions on ring D, additional substituents on ring A, and unsaturation of ring B decrease the affinity for the receptor while presence or absence of the angular methyl group on C-13 has no influence.
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