Isolation and characteristics of carboxypeptidase B from the pyloric ceca of the starfish Asterias amurensis.
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-L-arginine were at approximately pH 7.5 and 55 degrees C, respectively. The enzyme was unstable at above 50 degrees C and at below pH 5.0. The enzyme was activated by Co(2+), but was inhibited by EDTA and Hg(2+). The N-terminal amino acid sequence of A. amurensis carboxypeptidase B was ASFDYNVYHSYQEIMNWITN.
Kishimura
Hideki
H
Graduate School of Fisheries Sciences, Hokkaido University, Hakodate, Hokkaido 041-8611, Japan. kishi@fish.hokudai.ac.jp
Hayashi
Kenji
K
D000595:Amino Acid Sequence; D000818:Animals; D043424:Carboxypeptidase B; D002268:Carboxypeptidases / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D003035:Cobalt / Q000494:pharmacology; D004064:Digestive System / Q000201:enzymology; D004492:Edetic Acid / Q000494:pharmacology; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D008628:Mercury / Q000494:pharmacology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013215:Starfish / Q000201:enzymology*; D013696:Temperature
D003035:Cobalt; D004492:Edetic Acid; D002268:Carboxypeptidases; D043424:Carboxypeptidase B; D008628:Mercury