Method for promoting disulfide bond formation in recombinant proteins

摘要

Reduced cysteine-containing proteins consisting of recombinant IFN- beta , IL-2 or muteins thereof may be oxidized selectively so that the recombinant proteins have essentially the same disulfide bridging and biological activity as their native counterparts. The oxidized product is substantially free of unwanted side products and contains a minimal amount of intermolecular oligomers. The oxidation takes place in an aqueous medium containing a solubilizing agent at a pH of about 5.5 to 9, preferably at a pH of about 7. The reaction is initiated by addition of at least an effective amount of an oxidation promoter containing a Cu+2 cation such as CuCl2 or o-phenanthroline/Cu+2 complex in the presence of air.