Abstract
Sodium dodecyl sulfate gel electrophoresis revealed rapid proteolytic degradation of myosin heavy chain in heated arrowtooth flounder muscle. A proteolytic enzyme of approximately 32,000 molecular weight was extracted from the muscle and purified 125 fold. Activity of the semi-purified enzyme at 55°C was optimal against casein at pH 6.0-7.0. Incubation with chemical reagents indicated the involvement of sulfhydryl groups in enzyme activity.
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