Abstract
Investigations of fetal and placental tissues from monkeys and humans indicated that enzymes were present which could catalyze the conversion of naphthalene-1,2-oxide to the corresponding diol. Each of the tissues also exhibited measurable dihydrodiol dehydrogenase and glutathione S-epoxide transferase activities. Specific activities for epoxide hydrase were far lower in placental tissues than any of the other fetal tissues studied and also did not correlate with specific activities of aryl hydrocarbon hydroxylase. Human placentas from early gestation (10-18 weeks) displayed approximately 2-fold higher epoxide hydrase activities than those investigated at term. Hydroxylation of naphthalene could not be detected in human term placentas which exhibited aryl hydrocarbon hydroxylase activities of the same magnitude as those observed in adult rat livers. The human fetal kidney appeared to possess an unusually active epoxide hydrase system. Dihydrodiol dehydrogenase and glutathione S-epoxide transferase activities were higher in soluble fractions from most of the primate fetal tissues than in corresponding preparations from adult rat livers.
Footnotes
- Received March 25, 1974.
- Copyright © 1974 by The American Society for Pharmacology and Experimental Therapeutics
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