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Fusion Protein on Sumo Molecular Chaperone and Antifungal Peptide Drs Help to Soluble Expression |
Xiao Ye-Chen yuxiaqin qin xiejiasen xie liu xiaoju liu yangwanying yang |
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Abstract After Sumo molecular chaperone and Antifungal Peptide Drosomycin were synthesized by PCR, the recombinant plasmid pET-3c-SD was constructed successfully. After the recombinant plasmid was transformed into BL21(DE3), fusion proteins expressed in the E.coli 21 (DE3) by the induction of IPTG. Target proteins attained percent 80 in total proteins. Meantime, Soluble protein exceeds 80% in total target proteins. The fusion protein was purified by Ni-NTA affinity chromatography,and its purification exceeds percent Ninety-five. The experiment shows the fusion protein own the antifungal activity, and this construction strategy help to facilitate small molecular peptide expression that had several two disulfide bonds
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Received: 28 September 2007
Published: 25 December 2007
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