Fusion expression of cecropin X including the cleavage of FXa in Escherichia coli

PCR method was used to introduce the code sequence of Factor Xa cleavage site to the 5' end of cecropin CMIV mutant gene X, then the gene was cloned into the expression vector pGEX-KG, and was highly expressed in E. coli BL21 by IPTG induction. The fusion protein was purified by affinity-chroma...

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Bibliographic Details
Published inShengwu gongcheng xuebao Vol. 16; no. 3; p. 411
Main Authors Yuan, L D, Dou, F, Liang, Y P, Xie, W, Wang, F, Zhang, S Q, Dai, Z Y
Format Journal Article
LanguageChinese
Published China 01.05.2000
Subjects
Antimicrobial Cationic Peptides - biosynthesis
Antimicrobial Cationic Peptides - isolation & purification
Antimicrobial Cationic Peptides - pharmacology
Escherichia coli - genetics
Factor Xa - metabolism
Insect Hormones - biosynthesis
Recombinant Fusion Proteins - biosynthesis
Recombinant Fusion Proteins - isolation & purification
Recombinant Fusion Proteins - pharmacology
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Summary:PCR method was used to introduce the code sequence of Factor Xa cleavage site to the 5' end of cecropin CMIV mutant gene X, then the gene was cloned into the expression vector pGEX-KG, and was highly expressed in E. coli BL21 by IPTG induction. The fusion protein was purified by affinity-chromatography and was cleaved by Factor Xa. Cecropin X with antibacterial activity was obtained after purified by ion-exchange chromatography.
ISSN:1000-3061