High-Level Expression and Novel Purification Strategy of Recombinant Thanatin Analog in Escherichia coli

@article{Wu2008HighLevelEA,
  title={High-Level Expression and Novel Purification Strategy of Recombinant Thanatin Analog in Escherichia coli},
  author={G.-Q. Wu and Lin Li and J.-X. Ding and L.-Z. Wen and Z.-L. Shen},
  journal={Current Microbiology},
  year={2008},
  volume={57},
  pages={95-101}
}
Recombinant thanatin analog (TH1) is a cationic 20-amino-acid antibacterial peptide with a conserved cysteine disulfide bond. It exhibits a broad antibacterial spectrum. Different strategies have been developed to produce small antibacterial peptides using recombinant techniques. To date, no efforts to obtain large quantities of active recombinant TH1 have been reported. This study describes the synthesis of TH1 gene, the heterologous fusion expression of the peptide in Escherichia coli, and… CONTINUE READING

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