Improved Expression in Escherichia Coli and Stability of Halophilic β-Lactamase-Firefly Luciferase Fusion Protein
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- ISHIBASHI Matsujiro
- Applied and Molecular Microbiology, faculty of Agriculture, Kagoshima University
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- ARAKE Makoto
- Applied and Molecular Microbiology, faculty of Agriculture, Kagoshima University
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- TOKUNAGA Hiroko
- Applied and Molecular Microbiology, faculty of Agriculture, Kagoshima University
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- ARAKAWA Tsutomu
- Alliance Protein Laboratories
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- TOKUNAGA Masao
- Applied and Molecular Microbiology, faculty of Agriculture, Kagoshima University
書誌事項
- タイトル別名
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- Improved Expression in <I>Escherichia Coli</I> and Stability of Halophilic β-Lactamase-Firefly Luciferase Fusion Protein
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Halophilic bacteria living in high salinity environments, i.e., oceans, salt lakes salty foods, etc., produce halophilic enzymes that show high aqueous solubility, strong resistance to protein aggregation, and high refolding and renaturation efficiency. These properties are associated with their abundant net negative charges. Firefly (Photinus pyralis) luciferase is widely used in a variety of applications, but known as an aggregation-prone protein with low stability. Here, we demonstrated that halophilic β-lactamase confers to the firefly luciferase higher solubility and stability as a His-β-lactamase-luciferase fusion protein construct.
収録刊行物
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- 日本海水学会誌
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日本海水学会誌 68 (6), 341-343, 2014
日本海水学会
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詳細情報 詳細情報について
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- CRID
- 1390001204597548160
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- NII論文ID
- 130005097762
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- NII書誌ID
- AN0018645X
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- ISSN
- 21859213
- 03694550
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- NDL書誌ID
- 025961007
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- NDL
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可