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ID 47725
フルテキストURL
著者
Rajapakse, Sanath Laboratory of Molecular and Cellular Interactions, Faculty of Advanced Life Science, Hokkaido University
Ogiwara, Katsueki Laboratory of Molecular and Cellular Interactions, Faculty of Advanced Life Science, Hokkaido University
Yamano, Noriko Department of Biology, Faculty of Science, Okayama University
Kimura, Atsushi Laboratory of Molecular and Cellular Interactions, Faculty of Advanced Life Science, Hokkaido University
Hirata, Kensaku Department of Biology, Faculty of Science, Okayama University
Takahashi, Sumio Department of Biology, Faculty of Science, Okayama University
Takahashi, Takayuki Laboratory of Molecular and Cellular Interactions, Faculty of Advanced Life Science, Hokkaido University
抄録
Mouse tissue kallikreins (Klks) are members of a large, multigene family consisting of 37 genes, 26 of which can code for functional proteins. Mouse tissue kallikrein 5 (KIk5) has long been thought to be one of these functional genes, but the gene product, mK5, has not been isolated and characterized. In the present study, we prepared active recombinant mK5 using an Escherichia coli expression system, followed by column chromatography. We then determined the biochemical and enzymatic properties of purified mK5. mK5 had trypsin-like activity for Arg at the P1 position, and its activity was inhibited by typical serine protease inhibitors. mK5 degraded gelatin, fibronectin, collagen type IV, high-molecular-weight kininogen, and insulin-like growth factor binding protein-3. Our data suggest that mK5 may be implicated in the process of extracellular matrix remodeling.
キーワード
mouse
protease
kallikrein 5
recombinant enzyme
characterization
発行日
2006-11
出版物タイトル
Zoological Science
23巻
11号
出版者
Zoological Society of Japan
出版者(別表記)
日本動物学会
開始ページ
963
終了ページ
968
ISSN
0289-0003
NCID
AA10545874
資料タイプ
学術雑誌論文
言語
English
OAI-PMH Set
岡山大学
著作権者
© 2006 Zoological Society of Japan
論文のバージョン
publisher
査読
有り
DOI
PubMed ID
Web of Sience KeyUT