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
Kaken ID
publons
researchmap
Takahashi, Takayuki
Laboratory of Molecular and Cellular Interactions, Faculty of Advanced Life Science, Hokkaido University
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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.
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キーワード | mouse
protease
kallikrein 5
recombinant enzyme
characterization
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発行日 | 2006-11
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出版物タイトル |
Zoological Science
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巻 | 23巻
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号 | 11号
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出版者 | Zoological Society of Japan
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出版者(別表記) | 日本動物学会
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開始ページ | 963
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終了ページ | 968
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ISSN | 0289-0003
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NCID | AA10545874
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資料タイプ |
学術雑誌論文
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言語 |
英語
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著作権者 | © 2006 Zoological Society of Japan
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論文のバージョン | publisher
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査読 |
有り
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DOI | |
PubMed ID | |
Web of Science KeyUT |