Abstract
Myosin B from normal and PSE porcine muscles was studied by superprecipitation and SDS polyacrylamide gel electrophoresis. Similar studies were made on the fractions derived from the myosin B preparation after ultracentrifugation. Myosin B and its fractions from PSE muscle showed much less superprecipitation than normal. This difference between normal and PSE muscle seems to reflect differences in biological activity of their myofibrillar proteins, rather than differences in myofibrillar protein composition.
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