Abstract
Hydrolytic degradation of carp myosin with carp and rabbit calpains in 0.5M NaCl were followed by SDS-polyacrylamide gel electrophoresis and other methods. Carp myosin heavy chain was degraded restrictively into two subfragments (170, 000 and 43, 000 Mr proteins), carp calpain's activity being three times higher than rabbit calpain. In contrast, three light chains from this myosin were hardly degraded. Maximal hydrolysis as well as caseinolysis of this myosin occurred at lmM Ca+2 and at neutral pH. The hydrolysis showed an accelerated pace above 20°C. Rabbit myosin used for comparison was insusceptible to both calpains.The two subfragments thus produced from carp myosin were separated from each other by differences in solubility. The soluble subfragment was composed of 170, 000 Mr protein and three light chains, and the insoluble was composed of 43, 000 Mr protein. The soluble subfragment exhibited a Ca2+-ATPase activity similar to the original myosin and the Mg2+-ATPase activity was accelerated by F-actin. It was concluded that carp myosin is degraded by either calpain into heavy and light meromyosin-like subfragments.
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