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CHARACTERISTICS OF TWO TRYPSIN ISOZYMES FROM THE VISCERA OF JAPANESE ANCHOVY (ENGRAULIS JAPONICA)
Title: | CHARACTERISTICS OF TWO TRYPSIN ISOZYMES FROM THE VISCERA OF JAPANESE ANCHOVY (ENGRAULIS JAPONICA) |
Authors: | KISHIMURA, HIDEKI Browse this author →KAKEN DB | HAYASHI, KENJI Browse this author | MIYASHITA, YUSUKE Browse this author | NONAMI, YOSHIYUKI Browse this author |
Keywords: | Japanese anchovy | Engraulis japonica | Purification | Trypsin | Isozyme | Thermal stability |
Issue Date: | Oct-2005 |
Publisher: | Blackwell Publishing |
Journal Title: | Journal of Food Biochemistry |
Volume: | 29 |
Issue: | 5 |
Start Page: | 459 |
End Page: | 469 |
Publisher DOI: | 10.1111/j.1745-4514.2005.00029.x |
Abstract: | Two isozymes of trypsin (TR-I and TR-II) were purified from the viscera of Japanese anchovy (Engraulis japonica) by gel filtration and anion-exchange chromatography. Final enzyme preparations were nearly homogeneous in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and the molecular weights of both enzymes were estimated to be 24,000 Da by SDS-PAGE. The N-terminal amino acid sequences of the TR-I, IVGGYECQAHSQPHTVSLNS, and TR-II, IVGGYECQPYSQPHQVSLDS, were found. Both TR-I and TR-II had maximal activities at around pH 8.0 and 60C for hydrolysis of Nα-p-tosyl-L-arginine methyl ester hydrochloride. The TR-I and TR-II were unstable at above 50C and below pH 5.0 and were stabilized by calcium ion. |
Rights: | The definitive version is available at www.blackwell-synergy.com |
Relation: | http://www.blackwell-synergy.com |
Type: | article (author version) |
URI: | http://hdl.handle.net/2115/16938 |
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)
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Submitter: 岸村 栄毅
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