PDI-, PPI- and chaperone-catalyzed refolding of recombinant human IL-2 and GM-CSF.

Abstract

The studies on PDI-, PPI- and chaperone-catalyzed refolding of recombinant human IL-2 and GM-CSF show that PDI can prevent the mismatch of disulfide bonds and formation of aggregates by interchains linkage; furthermore, PDI can correct the mismatching of disulfide bonds in IL-2 isomers. PPI can increase the rate of folding reaction while chaperone can prevent the aggregation during the folding process. In addition, there is a synergistic effect between them.