Abstract
An enzyme that catalyzes the metabolism and binding of 14C-estradiol to protein, tyrosine and other substances in the presence of H 2O 2 was shown to be absent from the uteri of immature rats and to be induced by physiological doses of estrogen or pregnant-mare serum gonadotrophin. The characteristics of the uterine enzyme system as well as its subcellular distribution were determined and the effect of inhibitors was studied. The increase in the ability of uterine preparations to convert 14C-estradiol into water-soluble products as a result of estrogen treatment was accompanied by an increase in peroxidase and NADH oxidase activities and was inhibited by actinomycin D and cycloheximide. The nature of the water-soluble estrogen metabolites and the possible source of H 2O 2 was investigated. The results provide further evidence that estrogen metabolism occurs in estrogen-stimulated uteri and that it may be part of an adaptive response to limit the duration of action of this hormone upon its target tissue.
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