The metabolism of carbon tetrachloride has been investigated in liver microsomes and in reconstituted cytochrome P-450-dependent monooxygenase systems. In both cases cytochrome P-450 appears to be the sole site of carbon tetrachloride reduction. In aerobic incubations of microsomal preparations from phenobarbital-treated rats or rabbits, carbon tetrachloride induces large increases in NADPH oxidation and oxygen uptake. This cofactor utilization is not directly related to monooxygenase-mediated metabolism. Under aerobic conditions carbon tetrachloride induces lipid peroxidation, a reaction which is not inhibited by carbon monoxide. Under anaerobic conditions, carbon monoxide is a potent inhibitor of the cytochrome P-450-mediated reduction of carbon tetrachloride. These facts are inconsistent with a role for carbon tetrachloride metabolism in the potentiation of lipid peroxidation.
|Number of pages||6|
|Publication status||Published - 1 Dec 1980|