TY  - JOUR
T1  - Comparison of Three Methods for Refolding Recombinant Chicken Interleukin-18 Expressed in <I>E. coli</I>
AU - Kong, Na 
JO  - Journal of Animal and Veterinary Advances
VL  - 14
IS  - 1
SP  - 1
EP  - 5
PY  - 2015
DA  - 2001/08/19
SN  - 1680-5593
DO  - javaa.2015.1.5
UR  - https://makhillpublications.co/view-article.php?doi=javaa.2015.1.5
KW  - Artificial molecular chaperone
KW  -chicken IL-18
KW  -recombinant protein
KW  -inclusion bodies
KW  -protein refolding
AB  - 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.
ER  -