Localization of Proteolytic Activity in Muscle Protein Fractions

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Abstract
The myosin, myogen, globulin x, and myoalbumin protein fractions from the legs of the frog, Rana pipiens, were analyzed for the presence of the proteolytic enzymes, pepsin, trypsin, and cathepsin. Myogen was present in minute quantities and could not be separated from the myoalbumin fraction. The globulin x fraction did not show any proteolytic activity. For these reasons, the effect of the amt. of protein fraction on the amt. of proteolytic digestion and the effect of time on the amt. of proteolytic digestion was studied using a myosin and myosin-free fraction. Cathepsin and pepsin were localized in the myosin fraction and trypsin in the myosin-free fraction. Typical digestion curves were obtained. The myogen content of frog muscle is lower than that reported for mammals.

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