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Isolation and characteristics of carboxypeptidase B from the pyloric ceca of the starfish Asterias amurensis

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Title: Isolation and characteristics of carboxypeptidase B from the pyloric ceca of the starfish Asterias amurensis
Authors: Kishimura, Hideki Browse this author →KAKEN DB
Hayashi, Kenji Browse this author
Keywords: Asterias amurensis
Carboxypeptidase B
Isolation
Marine invertebrate
Metalloenzyme
N-terminal amino acid sequence
Pyloric cecum
Starfish
Issue Date: Oct-2002
Publisher: Elsevier Science Inc.
Journal Title: Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology
Volume: 133
Issue: 2
Start Page: 183
End Page: 189
Publisher DOI: 10.1016/S1096-4959(02)00130-6
Abstract: 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.
Relation: http://www.sciencedirect.com/science/journal/10964959
Type: article (author version)
URI: http://hdl.handle.net/2115/16937
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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