摘要
根据大肠杆菌的密码子偏好性,人工设计并合成了3条寡核苷酸片段,相邻片断有17个碱基的重叠区,通过PCR扩增得到抗菌肽Thanatin基因,将此基因克隆到原核表达载体pGEX-4T-1中,然后将重组质粒pGEX-Thanatin转化E.coliBL 21,经IPTG诱导进行融合表达。通过SDS-PAGE分析,融合蛋白GST-Thanatin表达成功。
Three gene fragments were designed and synthesized based on the preference of the codon of E. coli, and the gene of Thanatin was obtained by PCR amplification and cloned into prokaryotic expression vector pGEX-4T-1. Then the recombinant expression plasmid pGEX-Thanatin was transformed into E. coli BL21 and the fusion protein of Thanatin was produced by IPTG induction. The analysis of SDS - PAGE showed that the fusion pGEX- Thanatin protein was expressed, which might lay a foundation on research of antimicrobial activities and its mecha- nism.
出处
《安徽农业大学学报》
CAS
CSCD
北大核心
2007年第4期524-526,共3页
Journal of Anhui Agricultural University
