Abstract
Abstract Specific binding of 125 I-labeled human chorionic gonadotropin by receptors of the rat testis interstitial cells was not reduced by alkylation of the free -SH groups in particulate and solubilized receptor preparations. Reduction and alkylation of receptor disulfide groups abolished gonadotropin binding by uncharged receptor sites, but had no effect upon the retention of bound gonadotropin by preformed hormone-receptor complexes. Reduction and alkylation of gonadotropin also reduces subsequent binding of the hormone to testis receptors. These studies show that free -SH groups of testis receptors are not required for specific gonadotropin binding, whereas disulfide bonds form an important component of the receptor and appear to be essential for hormone-receptor interaction.
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