Soluble Expression of a Synthetic Gene for Human Translation Initiation Factor 4E in Escherichia coli
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概要
- 論文の詳細を見る
In order to obtain the active form of recombinant human initiation factor (eIF) 4E effectively, an artificial synthetic gene was cloned into an expression vector (pMAL-p2) and the soluble expression was attempted in Escherichia coli under the control of a tac promoter. Two expression systems were finally constructed as a fusion protein with maltose-binding protein, which contain a recognition sequence for the site specific protease α-thrombin and factor Xa, respectively. Most of the fusion protein was induced as a soluble form. The soluble human eIF-4E digested from the fusion protein showed binding specificity for the m^7GTP affinity column.
- 社団法人日本薬学会の論文
- 1995-02-15
著者
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上杉 晴一
Faculty Of Engineering Yokohama National University
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土井 光暢
大阪薬大
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石田 寿昌
大阪薬大
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石田 寿昌
大阪薬科大学
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寺岡 佳夏
大坂薬科大学 第二物理化学
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土井 充暢
Osaka University of Pharmaceutical Sciences
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石田 寿昌
Department of Physical Chemistry Osaka College of Pharmacy
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土井 光暢
Department of Physical Chemistry Osaka College of Pharmacy
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森野 重信
Department of Physical Chemistry, Osaka University of Pharmaceutical Sciences
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寺岡 佳夏
Department of Physical Chemistry, Osaka University of Pharmaceutical Sciences
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上田 仁司
Kawanishi Pharma Research Institute, Nippon Boehringer Ingelheim Co., Ltd.
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森野 重信
大坂薬科大学 第二物理化学
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石田 寿晶
大阪薬科大学
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Doi Mitsunobu
Department Of Physical Chemistry Osaka University Of Pharmaceutical Sciences
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上田 仁司
Kawanishi Pharma Research Institute Nippon Boehringer Ingelheim Co. Ltd.
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Uesugi S
Faculty Of Engineerign Yokohama National Unoversity
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