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Characteristics of carboxypeptidase B from pyloric ceca of the starfish:Asterina pectinifera

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Title: Characteristics of carboxypeptidase B from pyloric ceca of the starfish:Asterina pectinifera
Authors: Kishimura, Hideki Browse this author →KAKEN DB
Hayashi, Kenji Browse this author
Ando, Seiichi Browse this author
Keywords: Asterina pectinifera
Carboxypeptidase B
Marine invertebrate
Metalloenzyme
N-terminal amino acid sequence
Pyloric cecum
Starfish
Issue Date: Mar-2006
Publisher: Elsevier
Journal Title: Food Chemistry
Volume: 95
Issue: 2
Start Page: 264
End Page: 269
Publisher DOI: 10.1016/j.foodchem.2005.01.001
Abstract: Carboxypeptidase 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.
Relation: http://www.sciencedirect.com/science/journal/03088146
Type: article (author version)
URI: http://hdl.handle.net/2115/8371
Appears in Collections:水産科学院・水産科学研究院 (Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 岸村 栄毅

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