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Structural properties of trypsin from cold-adapted fish, arabesque greenling (Pleurogrammus azonus)

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Title: Structural properties of trypsin from cold-adapted fish, arabesque greenling (Pleurogrammus azonus)
Authors: Kanno, Gaku Browse this author
Kishimura, Hideki Browse this author →KAKEN DB
Ando, Seiichi Browse this author
Klomklao, Sappasith Browse this author
Nalinanon, Sitthipong Browse this author
Benjakul, Soottawat Browse this author
Chun, Byung-Soo Browse this author
Saeki, Hiroki Browse this author →KAKEN DB
Keywords: Trypsin
Pyloric caecum
Arabesque greenling
Pleurogrammus azonus
Primary structure
Thermostability
Cold-adaptation
Issue Date: Mar-2011
Publisher: Springer Berlin / Heidelberg
Journal Title: European Food Research and Technology
Volume: 232
Issue: 3
Start Page: 381
End Page: 388
Publisher DOI: 10.1007/s00217-010-1404-6
Abstract: A cDNA clone encoding trypsin (AG-T) was isolated from the pyloric ceca of cold-adapted fish, arabesque greenling (Pleurogrammus azonus). The cDNA was composed of 892 bp with an open reading frame of 729 bp at nucleotide positions 25-753. Similar to all the known trypsin, the AG-T seemed to be synthesized as preproenzyme that contains a hydrophobic signal peptide, an activation pentapeptide and a mature trypsin of 222 amino acid residues. The AG-T also completely conserved the major structural features common to trypsin such as the catalytic triad (His57, Asp102, and Ser195), the obligatory Asp189 and twelve Cys residues. On the other hand, the AG-T possessed the deletion of Tyr151 and substitution of Pro152 for Gly in the autolysis loop when aligned with the sequence of tropical-zone fish and bovine trypsins. In addition, Val75 concerned in a combination with calcium ion was exchanged for Ala in the AG-T, and the content of positively charged amino acid residues at the calcium-binding site of the AG-T was three times higher than those of tropical-zone fish trypsins. Moreover, the ratio between charged and hydrophobic amino acid residues in the N-terminal region of the AG-T was also higher than those of temperate-zone fish and tropical-zone fish trypsins. Such structural properties of the AG-T would contribute to its low thermostability.
Rights: The original publication is available at www.springerlink.com
Type: article (author version)
URI: http://hdl.handle.net/2115/48491
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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