Abstract
1. 1.The effects of CCl 4 on isolated lysosomes and rat-liver slices have been examined. The addition of CCl 4 to rat-liver lysosomes caused the release of β-glucuronidase, acid phosphatase, and acid ribonuclease activity. The release occurred without a lag period and was linear. In addition, the rate of release was found to be dependent on the CCl 4 concentration. 2. 2.CCl 4 added to liver slices caused a redistribution of the lysosomal enzyme activity such that a greater percentage was found in the supernatant versus the particulate fraction. Under these conditions [ 14C]leucine incorporation into protein was inhibited. The effects on lysosomal enzymes and on leucine incorporation were roughly comparable for a given concentration of CCl 4. Studies of the kinetics of these changes revealed both to be linear and to occur without any detectable lag period. 3. 3.Lysosomes were isolated by two different methods, such that lipid peroxidation occurred to a much greater extent in one preparation compared with the other. Despite this difference CCl 4 produced comparable release of lysosomal enzyme activity in both preparations. Furthermore, in neither lysosomal fraction was CCl 4 found to augment lipid peroxidation at a time when its effect on enzyme activity was maximal.
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