PubMed · 9016829
Does DsbA have chaperone-like activity?
Abstract
DsbA showed chaperone-like activity similar to but weaker than that of protein disulfide isomerase in increasing reactivation and decreasing aggregation during the refolding of guanidine hydrochloride-denatured D-glyceraldehyde-3-phosphate dehydrogenase and rhodanese. The fact that both enzymes are devoid of disulfide bonds indicates the independence of the chaperone-like activity of DsbA from its thiol-protein oxidoreductase activity. The increased reactivation of D-glyceraldehyde-3-phosphate dehydrogenase by DsbA can be suppressed with increasing concentrations of a peptide of 21 amino acid residues, suggesting that the peptide binding ability of DsbA is responsible for its chaperone-like activity.
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W D Zheng, H Quan, J L Song, S L Yang, C C Wang. 1997-01-15. Does DsbA have chaperone-like activity?. https://doi.org/10.1006/abbi.1996.9783
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