Isolation and characteristics of carboxypeptidase B from the pyloric ceca of the starfish Asterias amurensis
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Carboxypeptidase B was purified from the pyloric ceca of the starfish Asterias amurensis. The final enzyme preparation was nearly homogeneous in polyacrylamide gel electrophoresis and its molecular weight was estimated as approximately 34 000. The optimum pH and temperature of the enzyme for hydrolysis of benzoyl-glycyl--arginine were at approximately pH 7.5 and 55 °C, respectively. The enzyme was unstable at above 50 °C and at below pH 5.0. The enzyme was activated by Co2+, but was inhibited by EDTA and Hg2+. The N-terminal amino acid sequence of A. amurensis carboxypeptidase B was ASFDYNVYHSYQEIMNWITN.
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- Isolation and characteristics of carboxypeptidase B from the pyloric ceca of the starfish Asterias amurensis