CHARACTERISTICS OF TWO TRYPSIN ISOZYMES FROM THE VISCERA OF JAPANESE ANCHOVY (ENGRAULIS JAPONICA)

KISHIMURA, HIDEKI; HAYASHI, KENJI; MIYASHITA, YUSUKE et al.

Journal of Food Biochemistry, 2005, 29(5), 459-469

Permalink : https://hdl.handle.net/2115/16938

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アクセス権
open access
URI
https://hdl.handle.net/2115/16938
タイトル
CHARACTERISTICS OF TWO TRYPSIN ISOZYMES FROM THE VISCERA OF JAPANESE ANCHOVY (ENGRAULIS JAPONICA)
著者
KISHIMURA, HIDEKI ; HAYASHI, KENJI ; MIYASHITA, YUSUKE ; NONAMI, YOSHIYUKI
e-Rad_Researcher
50204855
著者名
KISHIMURA, HIDEKI
著者名
HAYASHI, KENJI
著者名
MIYASHITA, YUSUKE
著者名
NONAMI, YOSHIYUKI
言語
英語
キーワード
Japanese anchovy
Engraulis japonica
Purification
Trypsin
Isozyme
Thermal stability
発行日
2005-10
出版者
Blackwell Publishing
収録物名
Journal of Food Biochemistry
巻(号)
29(5)
ページ
459-469
抄録
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.
資源タイプ
学術雑誌論文
出版タイプ
Accepted Manuscript
権利情報
The definitive version is available at www.blackwell-synergy.com
PISSN
0145-8884
EISSN
1745-4514
関連情報
URI
http://www.blackwell-synergy.com
関連情報 (isVersionOf)
出版社版DOI
https://doi.org/10.1111/j.1745-4514.2005.00029.x