魚類筋タンパク質の変性に関する研究-1-冷凍変性コイ・アクトミオシンの物理化学的・電子顕微鏡的研究〔英文〕

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With a view to exploring the molecular nature of the freeze-denaturation of muscle proteins, a multi-aspect study was done on carp actomyosin including measurements of solubility, viscosity, ATP-response, salting-out behavior, ultracentrifugal behavior and electron-microscopical observations. The solubility and intrinsic viscosity of actomyosin decreased with the length of frozen storage and the ultracentrifugal patterns showed aggregation proceeding during frozen storage. However, the loss of ATP-response appearing early in frozen storage suggested the occurrence of either dissociation into actin and myosin or the loss of dissociating capacity on addition of ATP. Electron microscopical observations showed that, by freezing and frozen storage, actomyosin filaments are not only aggregated side-to-side and/or cross-wise but are entangled into net-like masses, which appear even in centrifuged supernatants after prolonged frozen storage. Salting-out analysis showed that combination of actin and myosin is generally preserved after frozen storage. It was proposed that during frozen storage, actomyosin filaments form net-worked masses through aggregation and entangling and become increasingly insoluble with the growth in net-work and particle size of the masses.
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