Chaperone‐Like Activity of Protein Disulfide‐Isomerase in the Refolding Of Rhodanese

• DOI: 10.1111/j.1432-1033.1995.0312e.x
• Publication Date: 2010-07-21T17:07:38Z
• Authors: Jiu‐li Song; Chih‐chen Wang
• Keywords: Rhodanese; Chaperone (clinical); Guanidine

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 thermal inactivation. The above‐mentioned properties displayed by completely satisfy the definition chaperone provide additional evidence to confirm hypothesis proposed previously [Wang, C. & Tsou, L. (1993) FASEB J. 7 , 1515–1517] that is both an enzyme a chaperone. Since contains no disulfide bonds, chaperone‐like activity acting on independent its activity.