1991 年 55 巻 10 号 p. 2467-2473
High hydrostatic pressures of 100 MPa to 300 MPa were applied to isolated myofibrils prepared from rabbit skeletal muscle to investigate the pressure-induced degradation of myofibrillar structure in the muscle.
A marked loss of the regular structure was observed in the phase-contrast image of the isolated myofibrils pressurized at 150 MPa, with further progress of the rupture of structure with increasing pressure applied. When exposed to pressures of 200 MPa or higher, clumping of the crushed myofibrils was observed. Electron microscopic studies of the pressurized myofibrils showed that the loss of M-line materials, rupture of I-filament, and the loss of the structural continuity with the loss of Z-line progressed in the myofibrils with increasing pressure applied. A sigmoidal relationship was obtained between the degree of solubilization and the intensity of the pressure applied to the isolated myofibrils. The electrophoretic analysis indicated that the amount and the species of the protein released from the myofibrils at each stage of the pressurization corresponded to the disruption of the ultrastructure in the myofibrils.
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