期刊
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
卷 76, 期 1, 页码 157-162出版社
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.110672
关键词
antimicrobial peptide; Rana chensinensis; soluble protein; affinity purification; antibacterial activity
类别
资金
- Natural Science Basic Research Plan of Shaanxi Province, China [SJ08-ZT08, 2009JQ3002]
- Fundamental Research Funds for Central Universities [GK200902030, GK200902031]
- LOFCS from Shaanxi Normal University [08103, 09051]
Antimicrobial peptides are effector molecules of the innate immunity of amphibians. Here, one antimicrobial peptide cDNA precursor, prepropalustrin-2CE3, from the tadpole of the Chinese brown frog Rana chensinensis was cloned. The coding sequence corresponding to the mature palustrin-2CE peptide was subcloned into pGEX-6p-1. The soluble GST-palustrin-2CE fusion protein was successfully expressed in the BL21(DE3)-pLysS strain at 16 C, and the proportion of the fusion protein reached 35%-39% of the total cellular protein. After removal of the GST-fusion tag, the purity of the palustrin-2CE obtained by Sephadex G50 chromatography was about 97%. Moreover, the purified palustrin-2CE displayed obviously inhibitory activities against the sensitive bacteria Staphylococcus aureus, Bacillus subtilis, Pseudomonas aeruginosa, and Escherichia coli, and multi-drug resistant S. aureus and E. coli. These findings suggest that the tadpole of the Chinese brown frog is a unique source of antimicrobial peptides and indicates the therapeutic potential of the palustrin-2CE peptide.
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