Na  Kong, 
    Comparison of Three Methods for Refolding Recombinant Chicken Interleukin-18 Expressed in <I>E. coli</I>,
    Journal of Animal and Veterinary Advances,
    Volume 14,Issue 1,
    2015,
    Pages 1-5,
    ISSN 1680-5593,
    javaa.2015.1.5,
    (https://makhillpublications.co/view-article.php?doi=javaa.2015.1.5)
    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.
    Keywords: Artificial molecular chaperone;chicken IL-18;recombinant protein;inclusion bodies;protein refolding