Renaturation of ovotransferrin under two-step conditions allowing primary folding of the fully reduced form and the subsequent regeneration of the intramolecular disulfides.

摘要: A two-step procedure was found to be useful for the efficient refolding of a complex protein, ovotransferrin. In first step, reduced and denatured form protein incubated at low temperature in nondenaturing buffer containing glutathione; second reoxidized higher presence oxidized glutathione. Under these conditions, fully forms ovotransferrin its half-molecules were almost quantitatively regain iron-binding abilities conformations, very similar native form. The circular dichroism spectra revealed that temperatures have partially folded which are fluctuating like "molten globule" states. reoxidization kinetics compared between whole two supported independent N- C-terminal domains.