Mechanism of postmortem autolysis of skeletal muscle.

Male Wistar rats were treated with the carboxyl, thiol, and serine protease inhibitors, pepstatin, Ep-475[L-trans-epoxysuccinyl-leucylamide(3-methyl) butane; E-64-c], and chymostatin. Then the femoral muscles of these rats and control animals were used for preparation of myofibril proteins. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis was used to analyze the degradation of these myofibril proteins with time (day) after death. The protease activities of the muscle were also measured. Tropomyosin was degraded most rapidly, followed by the heavy chain of myosin, alpha-actinin, and light chains of myosin (L1 and L2). Actin and troponin-T were degraded slowly, still remaining unchanged 2 weeks after death. The degradation of protein was not inhibited by pepstatin but was inhibited strongly by Ep-475 and very strongly by chymostatin. Chymostatin inhibited degradation of all components except alpha-actinin more strongly than Ep-475. Data on enzyme activities were consistent with these findings. These results suggest that after death the components of myofibrils are degraded with various proteases at various rates depending on their properties or their structure and that the proteases involved in the degradation show some specificity.