Bioactivation and hepatotoxicity of 2H/3H halothane

I. G. Sipes, A. J. Gandolfi

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Results in rats suggest that scission of the C-H bond is not a determining factor in the hepatotoxicity of halothane, since no apparent differences in liver injury were observed between halothane and d-halothane. Also, no significant changes between halothane and d-halothane were found in the levels of those metabolites produced during the reductive biotransformation of halothane (F- and the volatile metabolites, CDE and CTE). However, deuterium substitution markedly reduced the oxidative biotransformation of halothane, as evidenced by the 60% decrease in debromination. The covalent binding data also indicate that scission of the C-H bond does not occur during reductive bioactivation of halothane, since the 3H was retained under reductive conditions. The differences in stoichiometry of the binding of 3H-halothane and 14C-halothane are interesting and may indicate that different reactive intermediates exist for binding to lipid or protein and/or for O2 or N2 atmospheres, or reflect isotope effects or isotope exchange reactions. However, binding of 3H-halothane equivalents may be a useful marker for reductive biotransformation of halothane and its associated toxicity.

Original languageEnglish (US)
Pages (from-to)S242
Issue number3 SUPPL
StatePublished - 1979

ASJC Scopus subject areas

  • Anesthesiology and Pain Medicine


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