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Novel carbohydrate-binding activity of pancreatic trypsins to N-linked glycans of glycoproteins
http://hdl.handle.net/10083/458
http://hdl.handle.net/10083/45827fb2c95-8927-4f53-9d48-1aedc92ae60d
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
J. Biol. Chem 281(13).pdf (845.1 kB)
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| Item type | 学術雑誌論文 / Journal Article(1) | |||||
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| 公開日 | 2018-01-26 | |||||
| タイトル | ||||||
| タイトル | Novel carbohydrate-binding activity of pancreatic trypsins to N-linked glycans of glycoproteins | |||||
| 言語 | en | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源 | http://purl.org/coar/resource_type/c_6501 | |||||
| タイプ | journal article | |||||
| アクセス権 | ||||||
| アクセス権 | open access | |||||
| アクセス権URI | http://purl.org/coar/access_right/c_abf2 | |||||
| 著者 |
Takekawa, Hiroko
× Takekawa, Hiroko× Ina, Chieko× Sato, Reiko× Toma, Kazunori× Ogawa, Haruko |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | How glycosylation affects the reactivity of proteins to trypsin is not well understood. Bovine and porcine pancreatic trypsins were discovered to bind to α-Man, Neu5Acα2,6Galβ1,4Glc, and α-Gal sequences by binding studies with biotinylated sugar-polymers. Quantitative kinetic studies supported that phenylmethylsulfonyl fluoride (PMSF)-treated trypsin binds to glycolipid analogues possessing α-Man or α-NeuAc but not to those possessing β-Gal or β-GlcNAc residue. ELISA showed that trypsin binds to six kinds of biotinylated glycoproteins possessing high mannose-type and complex type N-glycans but not to bovine submaxillary mucin, which possesses only O-glycans. Further, the binding of trypsin to glycoproteins was differentially changed by treatments with sequential exoglycosidases, endoglycosidase H, or N-glycosidase F. Quantitative kinetic studies indicated that PMSF-treated trypsin binds with bovine thyroglobulin with the affinity constant of 1010 M-1, which was the highest among the glycoproteins examined, and that α-galactosidase treatment decreased it to 105 M-1. PMSF-treated trypsin bound to other glycoproteins inc\<br/>luding ovomucoid, a trypsin inhibitor, with the affinity constants of 108-105 mol-1 and were markedly changed by glycosidase treatments in manners consistent with the sugar-binding specificities suggested by ELISA. Thus, the binding site for glycans was shown to be distinct from the catalytic site, allowing trypsin to function as an uncompetitive activator in the hydrolysis of a synthetic peptide substrate. Correspondingly the carbohydrate-binding activities of trypsin were unaffected by treatment with PMSF or soybean trypsin inhibitor. The results indicate the presence of an allosteric regulatory site on trypsin that sugar-specifically interacts with glycoproteins in addition to the proteolytic catalytic site. | |||||
| 書誌情報 |
Journal of Biological Chemistry 巻 281, 号 13, p. 8528-8538, 発行日 2006-03-31 |
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| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 0021-9258 | |||||
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| 収録物識別子タイプ | NCID | |||||
| 収録物識別子 | AA00251083 | |||||
| 権利 | ||||||
| 権利情報 | Copyright (c) 2006 by the American Society for Biochemistry and Molecular Biology. | |||||
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| 内容記述タイプ | Other | |||||
| 内容記述 | text/plain | |||||
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| 内容記述タイプ | Other | |||||
| 内容記述 | application/pdf | |||||
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| 内容記述タイプ | Other | |||||
| 内容記述 | application/pdf | |||||
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| 内容記述タイプ | Other | |||||
| 内容記述 | text/plain | |||||
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| 出版タイプ | ||||||
| 出版タイプ | AM | |||||
| 出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||
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| 値 | author | |||||
| 日本十進分類法 | ||||||
| 主題Scheme | NDC | |||||
| 主題 | 464 | |||||
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| 主題Scheme | Other | |||||
| 主題 | 生物学 | |||||
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| 出版者 | The American Society for Biochemistry and Molecular Biology | |||||
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| 内容記述タイプ | Other | |||||
| 内容記述 | 学術雑誌論文 | |||||
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| 関連タイプ | isVersionOf | |||||
| 識別子タイプ | URI | |||||
| 関連識別子 | https://doi.org/10.1074/jbc.M513773200 | |||||
