Fusion expression of bovine lactoferricin in Escherichia coli
作者： Xing-jun Feng , Jian-hua Wang , An-shan Shan , Da Teng , Ya-lin Yang
DOI: 10.1016/J.PEP.2005.08.016
关键词:
摘要: The drug resistance problem has been growing with the utilization of current antibiotics in feed and medical industries. LfcinB, a 25-amino acid antibacterial peptide derived from bovine lactoferrin, is one potential alternatives antibiotics. According to bias codon Escherichia coli, fragment encoding LfcinB chemically synthesized, inserted into vector pGEX-4T-2 expressed E. coli. was fused GST protease cleavage site located between them. Two constructs different sites were made. One construct, pGEX-Th-LfcinB, contains thrombin carried by vector, other, pGEX-Th-Xa-LfcinB, Factor Xa which introduced after site. Fusion protein GST-Th-LfcinB efficiently cleaved thrombin, yielding recombinant showing activity. However, fusion GEX-Th-Xa-Lfcin B containing recognition could not be at conditions tried this study. Successful expression coli provides possible method produce large amounts.
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