Purification of the Ruminococcus albus Endoglucanase IV Using a Cellulose-Binding Domain as an Affinity Tag
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概要
- 論文の詳細を見る
The gene encoding the single cellulose-binding domain II (CBD II) of Clostridium stercorarium xylanase A was fused to the egIV gene enoding endoglucanase IV (EGIV) from Ruminococcus albus. The fusion protein (EGIV +CBDII) expressed in Esherichia coli can be readily purified from the cell-free extract of E. coli in a single step using the affinity of CBD to cellulose. The purified enzyme was claved into two moieties, i.e. the catalytic domain and CBD, at a specific site in the linker region by partial digestion with trypsin at 4℃. This result indicates that this CBD belongin to family VI of CBD families can be used as an affinity tag for purification of the recombinant protein.
- 公益社団法人日本生物工学会の論文
- 1997-10-25
著者
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Kajino T
Special Research Laboratory Ii Toyota Central R&d Laboratories Inc.
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Kimura Tetsuya
National Center For Seeds And Seedlings
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KARITA Shuichi
Center for Molecular Biology and Genetics Mie University
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Kimura Tetsuya
Laboratory of Applied Microbiology, Faculty of Bioresources, Mie University
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Sakka Kazuo
Laboratory of Applied Microbiology, Faculty of Bioresources, Mie University
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Ohmiya Kunio
Laboratory of Applied Microbiology, Faculty of Bioresources, Mie University
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