Abstract
ABSTRACT Actomyosin was partially purified from cold stored adductor muscles. During two days of storage the reduced viscosity and Mg2+-ATPase activity decreased about 30 and 50%, respectively. These changes were due neither to actomyosin dissociation nor to fragmentation of the major component of the complex. A gradual decrease in both parameters was observed thereafter up to the end of storage. Relative percentage of myosin and myosin/actin ratio significantly decreased (p < 0.01) and that of actin increased (p < 0.01) after the second day. These changes were related to a decrease in myosin heavy chain and could explain the slow decrease in reduced viscosity and ATPase activity after the second day. Expressible moisture accompanied the protein denaturation during storage.
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