Abstract
Carboxypeptidase A-like enzyme was purified from the crude enzyme solution prepared from the pyloric caeca of the starfish Asterias amurensis by gel filtration on Sephacryl S-200, followed by DEAE-cellulose column chromatography. The homogeneity of the enzyme was demonstrated by polyacrylamide gel electrophoresis. The molecular weight of the enzyme was estimated to be about 35, 000 by SDS-poly-acrylamide gel electrophoresis. The optimum pH and temperature of the enzyme for hydrolysis of benzoyl-glycyl-L-phenylalanine were at around pH 7.5 and 55°C, respectively, and the enzyme was stable below 50°C and at pH 6-11. This enzyme was not activated by the addition of CoCl2. However, the enzyme inactivated by EDTA was activated by the addition of ZnCl2 or CoCl2.
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