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酸性条件下における米糠トリプシンインヒビターの Asp (19)-Pro (20) 結合の開裂(B. 生活科学)
https://kpu.repo.nii.ac.jp/records/5451
https://kpu.repo.nii.ac.jp/records/54517bc06cce-f26d-4d50-ba58-48a90c0d318f
名前 / ファイル | ライセンス | アクション |
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KJ00000079577.pdf (621.2 kB)
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Item type | [ELS]紀要論文 / Departmental Bulletin Paper(1) | |||||
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公開日 | 2017-02-20 | |||||
タイトル | ||||||
言語 | ja | |||||
タイトル | 酸性条件下における米糠トリプシンインヒビターの Asp (19)-Pro (20) 結合の開裂(B. 生活科学) | |||||
その他(別言語等) | ||||||
その他のタイトル | The Cleavage of Asp (19)-Pro (20) Bond in Rice Bran Trypsin Inhibitor under Acidic Condition (B. LIVING SCIENCE) | |||||
言語 | en | |||||
言語 | ||||||
言語 | jpn | |||||
資源タイプ | ||||||
資源タイプ | departmental bulletin paper | |||||
著者 |
田代, 操
× 田代, 操× 牧, 善輔 |
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抄録(日) | ||||||
内容記述タイプ | Other | |||||
内容記述 | 米糠トリプシンインヒビター(RBTI)分子中のAsp (19)-Pro (20)結合の開裂が酸性pH下で非酵素的に生じた。このことは,pH3.0でのRBTIのインキュベーション,開裂したペプチド結合を有する修飾RBTIの単離,さらに修飾インヒビターの還元およびS-カルボキシメチル化によって得られたペプチドの分析などにより明らかにされた。修飾RBTIのトリプシン阻害活性は未修飾のものに比べ著しく低下しており,これはRBTI分子中のAsp (19)-Pro (20)結合の開裂により阻害活性部位周辺の立体構造に変動が生じたためであると考えられた。 | |||||
言語 | ja | |||||
抄録(英) | ||||||
内容記述タイプ | Other | |||||
内容記述 | The cleavage of Asp (19)-Pro (20) bond in rice bran trypsin inhibitor (RBTI) occurred non-enzymatically at an acid pH. This was proved by the experiments such as incubation of RBTI at pH 3.0,isolation of a modified RBTI containing a cleaved peptide bond, and chemical analyses of peptides obtained by reduction and S-carboxymethylation of the modified inhibitor. The trypsin inhibitory activity of the modified RBTI was dramatically weaker than that of native RBTI, suggesting that the cleavage of the Asp (19)-Pro (20) bond in RBTI caused a conformational change in the structure of a reactive-site region. | |||||
言語 | en | |||||
書誌情報 |
ja : 京都府立大学学術報告. 理学・生活科学 en : The scientific reports of the Kyoto Prefectural University. Natural science and living science 巻 39, p. 29-34, 発行日 1988-11-18 |
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雑誌書誌ID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AN00062300 | |||||
ISSN | ||||||
収録物識別子タイプ | PISSN | |||||
収録物識別子 | 0075739X |