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

Mingbo Xu, W Meng, Xiankai Ma

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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.

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What this paper is about

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.

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Available 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.

Key concepts: Chaperone (clinical), Chemistry, Disulfide bond, Recombinant DNA, Protein folding, Protein disulfide-isomerase, Biophysics, Folding (DSP implementation)

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PDI-, PPI- and chaperone-catalyzed refolding of recombinant human IL-2 and GM-CSF. — Research Paper | ScholarLens