熱安定性の異なる魚類ミオシンのカルパイン感受性の比較

概要

論文の詳細を見る
When myosins prepared from the skeletal muscles of seven different fish species and rabbit were incubated with calpain in the low salt solution at various temperatures, a myosin rod-like fragment (Mr= 150, 000 protein band on SDS-PAGE) was preferentially formed in all myosins examined and increased proportionally to the cleavage of myosin heavy chain. It was found that rabbit myosin, the most thermally stable of myosins was used, the most stable to proteolysis; and enhanced cleavage of fish myosins at lower temperatures. The calpain susceptibility of fish myosins was found to increase in species adapted to colder environmental temperatures. The apparent rate constants for cleavage of each myosin heavy chain at various temperatures were closely correlated with those for thermal inactivation of the ATPase of the same myosin, suggesting that the cleavage rates are a reflection of the conformational state in the head region, subfragment-1, of myosin molecule. Therefore, the stability of each myosin to thermal denaturation may be followed by this proteolysis.
日本水産學會の論文