Survey of Rabbit Skeletal Muscle Peptidases Active at Neutral pH Regions

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Abstract
A survey of oligopeptide hydrolases active at neutral pH regions responsible for increased free ammo acids on aging of high ultimate pH muscles were performed examining chromatographic behavior and substrate specificity of rabbit skeletal muscle extract. The DEAE‐cellulose chromatography of muscle extract revealed five major activity peaks respectively ascribable to a dipeptidase, an aminotripeptidase, an ammopeptidase, leucine aminopeptidase and the 160,000 dalton‐aminopeptidase purified previously by us. Since the 160,000 dahon‐ammopeptidase showed a broader substrate specificity than the two other aminopeptidases, it is most likely that this enzyme shares the largest part in the tetrapeptide hydrolysis in rabbit skeletal muscle at neutral pH regions.