Efficient purification of native recombinant proteins using proteases immobilized on cellulose(METHOD)
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概要
- 論文の詳細を見る
Cellulose binding domain (CBD) fusion protease was employed to digest the CBD fusion protein. After cleavage, the tag free target proteins can be separated from the CBD tag and CBD fusion protease which still adsorbed to the cellulose by centrifugation. The green fluorescent protein was efficiently purified using this method.
- 公益社団法人日本生物工学会の論文
著者
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Yang Bo
School Of Bioscience And Bioengineering South China University Of Technology
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Shen Yanfei
School Of Bioscience And Bioengineering South China University Of Technology
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Lan Dongming
School of Chemistry and Chemical Engineering, South China University of Technology
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Tai Yan
Guangdong Provincial Key Laboratory of Liver Disease Research, 3rd Affiliated Hospital of Sun Yat-Sen University
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Wang Fanghua
College of Light Industry and Food Sciences, South China University of Technology
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Wang Yonghua
College of Light Industry and Food Sciences, South China University of Technology
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Tai Yan
Guangdong Provincial Key Laboratory Of Liver Disease Research 3rd Affiliated Hospital Of Sun Yat-sen University
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Wang Yonghua
College Of Light Industry And Food Sciences South China University Of Technology
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Lan Dongming
School Of Chemistry And Chemical Engineering South China University Of Technology
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Wang Fanghua
College Of Light Industry And Food Sciences South China University Of Technology
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- Efficient purification of native recombinant proteins using proteases immobilized on cellulose(METHOD)
- Efficient purification of native recombinant proteins using proteases immobilized on cellulose