Abstract
The biochemical and physicochemical changes of myosin (myosin A), actomyosin (natural actomyosin), and actin after pressure treatment were investigated to elucidate the cause ofthe increased gel strength of pressurized actomyosin. Analysis of DNase I inhibition capacity of actomyosin demonstrated that in buffers containing 0.6 M KCl most of the actin in actomyosin was denatured by pressures of 150 MPa. However, at KCl concentrations greater than 0.6 M, a large part of actin in actomyosin was found to exist as the depolymerized form (native G-actin) after the release of pressure
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