Abstract
Summary Chlorinated naphthalenes with high chlorine content, Halowax 1014 and Halowax 1051 (containing 62 and 70 wt.−% Cl, respectively), were potent inducers of enzymes catalyzing drug hydroxylation or glucuronidation in rat liver. A single i.p. dose (100 mg/kg), given 7 days before assaying the enzyme activities, enhanced ethoxycoumarin deethylation 10-fold, benzo(a)pyrene hydroxylation 2 – 5 -fold, and glucuronidation of 4-methylumbelliferone and 2-aminophenol 5-fold. The increases in enzyme activities were dose-dependent. The hydroxylation and glucuronidation reactions achieved maximal rates in one week, and they were still above control levels after one month. Chlorinated terphenyls as well as chloronaphthalenes with low chlorine content enhanced only slightly hydroxylation and glucuronidation reactions. The activities of epoxide hydratase and glutathione S-transferase were not altered after treatment of animals either with chloronaphthalenes or with chloroterphenyls.
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