Fig 9.

Refolding of lysozyme in the absence ($●$) and presence of ($●$) heated (A, B) and ($●$) oxidized (C, D) artemin. Denatured lysozyme (10 mg/mL) in a solution containing 40 mM DTT, 6 M GdmCl, and 50 mM potassium phosphate buffer, pH 7.1, was diluted with a mixing ratio of 1:50 by the refolding buffer. The diluted sample contained 13.89 μM lysozyme, 0.8 mM DTT, 0.12 mM GdmCl, and 50 mM potassium phosphate buffer, pH 8.5, 5 mM GSH, 5 mM GSSG, and 0.5 (A, C) and 1 μg/mL (B, D) artemin. The kinetic of refolding was recorded by monitoring light scattering at 400 nm at 25°C.