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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 | 2010/05 |
| 形態種別 | 研究論文（学術雑誌） |
| 査読 | 査読あり |
| 標題 | High solubility supports efficient refolding of thermally unfolded beta-lactamase. |
| 執筆形態 | 共著 |
| 掲載誌名 | Int J Biol Macromol. |
| 掲載区分 | 国内 |
| 巻・号・頁 | 47,pp.706-709 |
| 著者・共著者 | Arakawa T, Tokunaga H, Yamaguchi R, Tokunaga M |
| 概要 | Fusion technology is widely used to enhance soluble expression of recombinant proteins. We have shown before that halophilic β-lactamase (BLA) is an ideal candidate as a fusion partner. Here we have examined its thermal unfolding and refolding as a function of salt concentration. The thermal stability significantly increased as the salt concentration was increased from 0.2 to 1.84 M. Conversely, while reversibility of thermal unfolding was high at least up to 0.65 M salt, it was largely lost at 1.84 M. This was due to aggregation of thermally unfolded BLA. The addition of 3M urea suppressed aggregation, which in turn resulted in restoration of reversible refolding of heat-denatured protein. |