title: 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.
authors.affiliation: Institute of Basic Medical Sciences, Beijing, China.
authors.forename: M
authors.initials: M
authors.lastname: Xu
authors.forename: W
authors.initials: W
authors.lastname: Meng
authors.forename: X
authors.initials: X
authors.lastname: Ma
mesh_terms: D000591:Amino Acid Isomerases; D002352:Carrier Proteins; D002384:Catalysis; D018835:Chaperonin 10; D018834:Chaperonin 60; D016178:Granulocyte-Macrophage Colony-Stimulating Factor / Q000737:chemistry*; D006801:Humans; D007376:Interleukin-2 / Q000737:chemistry*; D007535:Isomerases; D019696:Peptidylprolyl Isomerase; D019704:Protein Disulfide-Isomerases; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D002352:Carrier Proteins; D018835:Chaperonin 10; D018834:Chaperonin 60; D007376:Interleukin-2; D011994:Recombinant Proteins; D016178:Granulocyte-Macrophage Colony-Stimulating Factor; D007535:Isomerases; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase; D019704:Protein Disulfide-Isomerases