Abstract
The insoluble inclusion bodies of soluble leukemia inhibitory factor receptor fusion protein (gp 190 sol DAF ) was solubilized in 8 M urea on the unfolding transitions, and several factors on the aggregate formation were indirectly analyzed for the refolding of gp 190 sol DAF. Results indicate that the refolding yield can be considerably increased at lowering concentration of the unfolding protein, a little soluble protein with the slow refolding appears in the process of the aggregate formation and the concentration of the denaturant must be down to a minimum level for its refolding.
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Liu, H., Moreau, JF., Gualde, N. et al. Refolding of soluble leukemia inhibitory factor receptor fusion protein (gp 190 sol DAF) from urea. Mol Cell Biochem 169, 43–50 (1997). https://doi.org/10.1023/A:1006890627639
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DOI: https://doi.org/10.1023/A:1006890627639