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Variety of Effect of n-Alcohols on Microenvironment of Some Proteases in Peptide Synthesis or Z (N-Benzyloxycarbonyl) : Amino Acid Ester Hydrolysis
http://hdl.handle.net/10091/845
http://hdl.handle.net/10091/8450adb3600-9355-43b3-9843-8056e0c08487
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
v32_03.pdf (345.3 kB)
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| Item type | 学術雑誌論文 / Journal Article(1) | |||||||||||
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| 公開日 | 2007-12-28 | |||||||||||
| タイトル | ||||||||||||
| タイトル | Variety of Effect of n-Alcohols on Microenvironment of Some Proteases in Peptide Synthesis or Z (N-Benzyloxycarbonyl) : Amino Acid Ester Hydrolysis | |||||||||||
| 言語 | ||||||||||||
| 言語 | eng | |||||||||||
| キーワード | ||||||||||||
| 主題 | protease, microenvironment, thermolysin, α-chymotrypsin, papain, pepsin | |||||||||||
| 資源タイプ | ||||||||||||
| 資源 | http://purl.org/coar/resource_type/c_6501 | |||||||||||
| タイプ | journal article | |||||||||||
| その他（別言語等）のタイトル | ||||||||||||
| その他のタイトル | ペプチド合成またはＺ(ベンジルオキシカルボニル） : アミノ酸エステル加水分解における２，３のプロテアーゼの微環境へのｎ-アルコール効果の多様性 | |||||||||||
| 言語 | ja | |||||||||||
| 著者 |
Sato, K
× Sato, K
× Tadasa, K
× Kayahara, H
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| 出版者 | ||||||||||||
| 出版者 | 信州大学農学部 | |||||||||||
| 引用 | ||||||||||||
| 内容記述 | 信州大学農学部紀要. 32(1-2): 15-22 (1995) | |||||||||||
| 書誌情報 |
信州大学農学部紀要 巻 32, 号 1-2, p. 15-22, 発行日 1995-12-31 |
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| 抄録 | ||||||||||||
| 内容記述 | To investigate the interaction of proteases (thermolysin, α-chymotrypsin, papain and pepsin) with organic solvent molecules, buffer systems in which n-alcohols were dissolved as to make a one-phase medium were used in the case of peptide synthesis or Z-amino acid hydrolysis as model reactions. The chain length of n-alcohols gave different characteristics of the effective patterns to the enzymes, and also each protease was affected in different modes of effective profiles by n-alcohols. Activity of α-chymotrypsin was increased by n-alcohols higher than n-hexanol grdually with increase of their concentration just over the saturation to the buffer. The activation was proposed to be non-essential by kinetics. Meanwhile, n-pentanol to α-chymotrypsin showed to be an uncompetitive inhibitor. | |||||||||||
| 資源タイプ（コンテンツの種類） | ||||||||||||
| ISSN | ||||||||||||
| 収録物識別子タイプ | ISSN | |||||||||||
| 収録物識別子 | 0583-0621 | |||||||||||
| 書誌レコードID | ||||||||||||
| 収録物識別子タイプ | NCID | |||||||||||
| 収録物識別子 | AN00121352 | |||||||||||
| 出版タイプ | ||||||||||||
| 出版タイプ | VoR | |||||||||||
| 出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||||||||
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Cite as
Sato, K, Tadasa, K, Kayahara, H, 1995, Variety of Effect of n-Alcohols on Microenvironment of Some Proteases in Peptide Synthesis or Z (N-Benzyloxycarbonyl) : Amino Acid Ester Hydrolysis: 信州大学農学部, 15–22 p.
