@article{MAKHILLJAVA20151414453,
    title = {Comparison of Three Methods for Refolding Recombinant Chicken Interleukin-18 Expressed in <I>E. coli</I>},
    journal = {Journal of Animal and Veterinary Advances},
    volume = {14},
    number = {1},
    pages = {1-5},
    year = {2015},
    issn = {1680-5593},
    doi = {javaa.2015.1.5},
    url = {https://makhillpublications.co/view-article.php?issn=1680-5593&doi=javaa.2015.1.5},
    author = {Na},
    keywords = {Artificial molecular chaperone,chicken IL-18,recombinant protein,inclusion bodies,protein refolding},
    abstract = {It has been proved that artificial chaperone-assisted protein refolding can promote the refolding of chemically denatured proteins via the sequential addition of low molecular weight &#147;artificial chaperones&#148;. The aim of the present study was to compare three methods for refolding recombinant Chicken IL-18 protein (rChIL-18) expressed in <I>E. coli</I>. The recombinant chicken IL-18 protein was efficiently expressed in inclusion bodies in the <I>E. coli</I> expression system. The inclusion bodies were thoroughly denatured with 6 M of Guanidine Hydrochloride (GH) and refolded by using the methods of artificial chaperone-assisted refolding, GH-deionized
water diafiltration and GH-glutathione renaturation. Results of our comparative studies demonstrated that refolding yield of rChIL-18 was at least two times higher using the method of artificial chaperone-assisted refolding (42.45%) than those using GH-deionized water diafiltration (10.67%) and GH-glutathione renaturation (14.83%). The optimal SI values were observed at different concentrations of rChIL-18 proteins refolded by the methods of artificial chaperone-assisted refolding (150 &mu;g L<SUP>-1</SUP>), GH-deionized water diafiltration (600 &mu;g L<SUP>-1</SUP> and GH-glutathione renaturation (400 &mu;g L<SUP>-1</SUP>). In conclusion, the method of artificial chaperone-assisted refolding is more efficient for the refolding of recombinant chicken IL-18 than those of GH-glutathione
renaturation and GH-glutathione renaturation.}
    }