The efficient expression of anti-HBsAg human Fd and L chain in E.coli / 中国免疫学杂志

ABSTRACT

Objective:Choosing efficient expression vector express anti HBsAg Fd and L chain in E.coli to produce anti HBsAg human Fab.Purificating inclusion bodies to denaturating and refolding the protein.Methods:Expression vector of PQE32 Fd、PQE32 L was constructed and transformed into E.coli strain M15,efficient expression clone was screened by SDS PAGE.Results:After induced by IPTG,M15 PQE32 Fd、M15 PQE32 L expressed insoluble recombinant protein in inclusion bodies.The Fd、L chain gene sequence conform with that reported in NCBI BLAST.Conclusion:The M15 PQE32 expression system is stable and efficient for expressing anti HBs human Fd、L chain.The denaturation and protein refolding of the anti HBsAg Fab expressed in inclusion bodies need to be studied further.