Chaperone-Like Activity of Protein Disulfide-Isomerase in the Refolding Of Rhodanese
- 1 July 1995
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 231 (2), 312-316
- https://doi.org/10.1111/j.1432-1033.1995.tb20702.x
Abstract
Protein disulfide-isomerase (PDI) in near stoichiometric concentrations promotes reactivation and prevents aggregation of guanidine-hydrochloride-denatured rhodanese during refolding upon dilution. PDI also suppresses aggregation of rhodanese during thermal inactivation. The above-mentioned properties displayed by PDI completely satisfy the definition of chaperone and provide additional evidence to confirm the hypothesis proposed previously [Wang, C. C. & Tsou, C. L. (1993) FASEB J. 7, 1515-1517] that PDI is both an enzyme and a chaperone. Since rhodanese contains no disulfide bonds, the chaperone-like activity of PDI acting on rhodanese is independent of its disulfide-isomerase activity.Keywords
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