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ヤマグチ ルイ
Rui Yamaguchi
山口 類 所属 熊本保健科学大学 保健科学部 医学検査学科 熊本保健科学大学大学院 保健科学研究科 保健科学専攻 職位 准教授 |
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| 言語種別 | 英語 |
| 発行・発表の年月 | 2013/07 |
| 形態種別 | 研究論文（学術雑誌） |
| 査読 | 査読あり |
| 標題 | Structure of Starch Binding Domains of Halophilic Alpha-Amylase at Low pH. |
| 執筆形態 | 共著 |
| 掲載誌名 | Protein Pept Lett. |
| 掲載区分 | 国内 |
| 巻・号・頁 | 20,pp.755-760 |
| 総ページ数 | 5 |
| 担当区分 | 筆頭著者 |
| 著者・共著者 | Yamaguchi R, Ishibashi M, Tokunaga H, Arakawa T, Tokunaga M. |
| 概要 | The solubility and structural properties of halophilic proteins are ascribed to their abundant acidic residues, resulting in large net negative charges at neutral pH. This study examined the effects of low pH, i.e., reduction of net negative charges on the structural properties of starch binding domain (SBD) of halophilic Kocuria varians α-amylase. Titration to pH 2.1 caused loss of 233 nm peak characteristic of aromatic interactions present in the native SBD at neutral pH and resulted in the spectrum with a 216 nm valley characteristic of β-sheet. The low pH β-sheet structure was stable against heat treatment. The addition of NaCl and trifluoroethanol resulted in decrease and increase of the 216 nm signal, without altering the spectral shape. These structural properties were significantly different from those of the native protein. |