2024-03-29T01:08:36Zhttps://eprints.lib.hokudai.ac.jp/dspace-oai/requestoai:eprints.lib.hokudai.ac.jp:2115/83712022-11-17T02:08:08Zhdl_2115_20049hdl_2115_141Characteristics of carboxypeptidase B from pyloric ceca of the starfish:Asterina pectiniferaKishimura, HidekiHayashi, KenjiAndo, SeiichiAsterina pectiniferaCarboxypeptidase BMarine invertebrateMetalloenzymeN-terminal amino acid sequencePyloric cecumStarfish464Carboxypeptidase B was purified from the pyloric ceca of the starfish Asterina pectinifera. The final enzyme preparation was nearly homogeneous in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and its molecular weight was estimated as approximately 34,000. The value of the specificity constant (kcat/Km) for hydrolysis of benzoyl-glycyl-L-arginine by the purified enzyme was 1.72×10^5 M^-1sec^-1. The optimal pH and the optimal temperature of the enzyme were pH 7.5 and 55 ℃, respectively. The enzyme was unstable above 50 ℃ and below pH 5.0. The enzyme was activated by Co2+, and inhibited by EDTA. The N-terminal amino acid sequence of the enzyme was determined as ATFDYNKYHSYQEIMDWVTN.ElsevierJournal Articleapplication/pdfhttp://hdl.handle.net/2115/8371https://eprints.lib.hokudai.ac.jp/dspace/bitstream/2115/8371/1/Kishimura.pdf0308-8146Food Chemistry9522642692006-03enginfo:doi/10.1016/j.foodchem.2005.01.001author