›› 2003, Vol. 46 ›› Issue (1): 114-117.
• RESEARCH PAPERS • Previous Articles Next Articles
WENG Hong-Biao1, 2, NIU Bao-Long2, MENG Zhi-Qi2*, XU Meng-Kui1
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Abstract: The thanatin gene was obtained and inserted into expression vector pGEX-3X by a DNA recombinant method which was checked by nucleotide sequencing. The fusion protein of GST-thanatin was produced by IPTG induction in Escherichia coli (BL21). The expression level was about 20%. The fusion protein was purified by GST affinity hromatography and digested by enterokinase. Partly purified with Sephadex G-25, the final product, thanatin exhibited antimicrobial activity.
Key words: GST fusion expression, Escherichia coli
WENG Hong-Biao1, 2, NIU Bao-Long2, MENG Zhi-Qi2*, XU Meng-Kui1. Cloning and fusion expression of the antimicrobial peptide thanatin gene in Escherichia coli[J]., 2003, 46(1): 114-117.
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