A chaperone‐mimetic effect of serum albumin on rhodanese

Rebecca Jarabak, John Westley, Joseph M. Dungan, Paul Horowitz

Research output: Contribution to journalArticlepeer-review

19 Scopus citations


Reactivation of denatured rhodanese (thiosulfate:cyanide sulfurtransferase, EC was found to be aided by the presence of serum albumin. Both the rate and the extent of reactivation of the urea‐denatured enzyme were optimal at low rhodanese and moderate serum albumin concentrations. Similarly, stabilization of the sulfurtransferase activity of rhodanese that had been partially unfolded at 40°C was aided by the presence of serum albumin. All the observations are in accord with a model in which enzyme that has been partially refolded from the urea‐denatured state or partially unfolded thermally interacts directly with serum albumin in a way that prevents rhodanese self‐association. Serum albumin thus acts as a molecular chaperone in these systems.

Original languageEnglish (US)
Pages (from-to)41-48
Number of pages8
JournalJournal of Biochemical Toxicology
Issue number1
StatePublished - Mar 1993
Externally publishedYes


  • Chaperone Effect
  • Cyanide Detoxication
  • Molten Globule Forms
  • Rhodanese Folding
  • Serum Albumin

ASJC Scopus subject areas

  • Toxicology


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