Effects of the protein disulfide isomerase on the refolding of recombinant proteins in vitro
Mingbo Xu, Meng Wenhua, Xiankai Ma
Abstract
Mingbo Xu, Meng Wenhua, Xiankai Ma
Abstract
To increase ratio of correctly folded recombinant proteins, the protein disulfide isomerase (PDI) was purified from bovine liver, and the effects of enzyme catalyzed refolding process were studied. The results indicate that the correct folding ratio of IL-2 increased from 30% to 58% under the action of equal molar of PDI, with the specific activity of IL-2 increased from 4×10~(6)u/mg to 8.2×10~(6)u/mg. PDI can also partially correct the mismatched IL-2 molecules to the correct folding status and further more, PDI can prevent the formation of oligomer due to interchain disulfide bonds. With similar mechanism, PDI can increase the specific activity of GM-CSF.
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To increase ratio of correctly folded recombinant proteins, the protein disulfide isomerase (PDI) was purified from bovine liver, and the effects of enzyme catalyzed refolding process were studied. The results indicate that the correct folding ratio of IL-2 increased from 30% to 58% under the action of equal molar of PDI, with the specific activity of IL-2 increased from 4×10~(6)u/mg to 8.2×10~(6)u/mg. PDI can also partially correct the mismatched IL-2 molecules to the correct folding status and further more, PDI can prevent the formation of oligomer due to interchain disulfide bonds. With similar mechanism, PDI can increase the specific activity of GM-CSF.
Key concepts: Protein disulfide-isomerase, Chemistry, Disulfide bond, Recombinant DNA, Isomerase, Foldase, Oligomer, Protein folding