Purification and Specificity of Carboxypeptidase from Streptomyces griseus K-1

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Abstract
A carboxypeptidase of St. griseus K-1 (CPase S) was found to possess the specificities of both mammalian pancreatic CPase A and B. Three adsorbents for affinity chromatography were prepared by coupling L-Leu, D-Leu, and D-Arg with CH-Sepharose 4B. D-Arg-CH-Sepharose and L-Leu-CH-Sepharose retained the purified CPase S but D-Leu-CH-Sepharose did not. The activities of CPase S toward CGL and BGA were eluted in the same position. CPase S migrated as a single band on polyacrylamide gel electrophoresis and the two activities were both extracted from this band on the gel.

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