Prokaryotic Expression of Alpha Fetoprotein and Optimization of Renaturation

doi:10.13560/j.cnki.biotech.bull.1985.2015.01.029

Abstract

Abstract: Plasmid pET32a-AFP was constructed to express recombinant human alpha fetoprotein, which was in the form of inclusion body, and the protein was obtained after renaturing optimization. The recombinant plasmid pET32a-AFP was transformed in E.coli, after induced by IPTG and purified by affinity column, the inclusion body was renatured under different conditions, including renature method, pH and addictives. The results showed that it had the highest renature efficiency when 1.0 mg/ml AFP was processed under one-step dialysis renature method and the pH is 8.5, with 0.5 mol/L L-Arg. This renature process made the recombinant AFP protein having the highest efficiency and easy to manipulate.

Key words: alpha-fetoprotein, prokaryotic expression, renaturation

Cai Lei, Jiao Liyuan, Wang Jihua, Tang Shixing. Prokaryotic Expression of Alpha Fetoprotein and Optimization of Renaturation[J]. Biotechnology Bulletin, 2015, 31(1): 193-197.

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