Purification and Further Characterization of Enteropeptidase from Porcine Duodenum.
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概要
- 論文の詳細を見る
Enteropeptidase [EC 3. 4. 21. 9] is a membrane-bound serine endopeptidase present in the duodenum that converts trypsinogen to trypsin. We previously cloned the cDNA of the porcine enzyme and deduced its entire amino acid sequence [M. Matsushima et al. (1994) J. Biol. Chem. 269, 19976-19982]. In the present study, we purified the porcine enzyme approximately 2, 200-fold in a 12% yield from a duodenal mucosal extract to apparent homogeneity by an improved procedure comprising four steps of chromatography including benzamidine-Sepharose affinity chromatography. Lectin blotting analysis suggested that the enzyme is glycosylated mainly with N-linked carbohydrate chains of the tri- and/or tetraantennary complex type. The H and L chains of the enzyme were separated into two major bands upon SDS-PAGE under reducing conditions, suggesting that the enzyme mainly comprises two isoforms, a higher molecular weight form and a lower molecular weight form. The enzyme was also separated by lectin affinity chromatography into two major fractions, named isoforms I and II, which corresponded to the higher and lower molecular weight forms, respectively. These two isoforms appeared to be different only in the carbohydrate moiety, having essentially the same enzymatic properties. The enzyme was optimally active at pH 8.0 toward Gly-Asp-Asp-Asp-Asp-Lys-β-naphthylamide, and was inhibited strongly by various serine proteinase inhibitors. Furthermore, it was also strongly inhibited by E-64 [L-trans-epoxysuccinyl-leucylamide-(4-guanido)-butane], a cysteine proteinase inhibitor. Substrate specificity studies involving various synthetic peptides indicated that acidic residues at the P2, P3, and/or P4 positions are especially favorable for maximal activity, but are not absolutely necessary, at least in the cases of peptide substrates.
- 社団法人 日本生化学会の論文
著者
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MIKI kazumasa
Department of Biology, Faculty of Science. Kanagawa University
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Omata Masao
Department Of Cardiology Narita Red Cross Hospital
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Yahagi Naohisa
Department Of Applied Physics Faculty Of Science Science University Of Tokyo
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Ichinose Masao
Department Of Chemistry Faculty Of Science Tokai University
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Inoue Hideshi
Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo
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Athauda Senarath
Department Of Biochemistry Faculty Of Medicine University Of Peradeniya
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Tsuchiya Yuichi
Department Of Biochemistry Toho University School Of Medicine
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Matsushima Masashi
Department Of Internal Medicine Tokai University School Of Medicine
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Sakurai Yasuko
Department Of Biophysics And Biochemistry Graduate School Of Science University Of Tokyo
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Ito Hisashi
Department Of Chemistry And Biological Science
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Takahashi Takayuki
Department Of Biophysics And Biochemistry Graduate School Of Science University Of Tokyo
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Kim Yong-Tae
Department of Chemistry, College of Science and Engineering, Aoyama Gakuin University
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Kim Yong-Tae
Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo
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Tsukada-Kato Shinko
Department of Internal Medicine, Faculty of Medicine
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Takahashit Kenji
Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo
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