Hq. Liu et al., REFOLDING OF SOLUBLE LEUKEMIA INHIBITORY FACTOR-RECEPTOR FUSION PROTEIN (GP-190 SOL DAF) FROM UREA, Molecular and cellular biochemistry, 169(1-2), 1997, pp. 43-50
The insoluble inclusion bodies of soluble leukemia inhibitory factor r
eceptor fusion protein (gp 190 sol DAF) was solubilized in 8 M urea on
the unfolding transitions, and several factors on the aggregate forma
tion were indirectly analyzed for the refolding of EP 190 sol DAF. Res
ults indicate that the refolding yield can be considerably increased a
t lowering concentration of the unfolding protein, a little soluble pr
otein with the slow refolding appears in the process of the aggregate
formation and the concentration of the denaturant must be down to a mi
nimum level for its refolding.