Release of phenyl acetate esterase from liver microsomes by carbon tetrachloride

Abstract

Decrease in phenyl acetate esterase activity of the microsomal fraction of mouse liver was observed within 6 h after intraperitoneal administration of carbon tetrachloride, in contrast to an increase both in the postmicrosomal supernatant (cytosol) fraction and in the serum. Incubation of microsomes with carbon tetrachloride was found to result in the release of the esterase activity into the medium, and the amount of the enzyme in the medium roughly paralleled the degree of lipoperoxidation. An adequate amount of ascorbic acid was also shown to be capable to induce in vitro lipoperoxidation, as well as the the release of enzyme. Inhibition of lipoperoxidation blocked the release of phenyl acetate esterase concomitantly. From these results, it may be suggested that carbon tetrachloride damages the microsomal membrane through lipoperoxidation resulting in phenyl acetate esterase release. This mechanism contributes at least in part to the decrease in activity of this enzyme in the liver which occurs 24 to 48 h after carbon tetrachloride treatment.