ABSTRACT
The recombinant plasmid of mChlL-18 prokaryotic expression was transformed into E.coli BL21(DE3) strain and then induced by IPTG at 37℃.After crushed and washed,the expressing inclusion bodies were thoroughly denatured with 6 mol/L guanidine hydrochloride.Then according to experiment design,the effects of rChlL-18 protein refolding yield at different densities were investigated by the systems of artificial chapercne at different densities.Experiment results indicate that there is a optimal condition on assiting rChIL-18 protein by using the artificial chaperone technique.The optimal condition can improve the refolding yield of rChIL-18 protein,and then the expressed product of fusion chicken IL-18 gene in E.coli has a relativity high bioactivity.