title: The unfolding and refolding of pig heart fumarase.
abstract: The unfolding of pig heart fumarase in solutions of guanidinium chloride (GdnHCl) has been examined. Loss of activity occurs at lower concentrations of GdnHCl than the structural changes detected by fluorescence or c.d. After denaturation, regain of activity can be observed provided that a reducing agent (dithiothreitol) is present and that the concentration of GdnHCl is lowered by dialysis rather than by dilution. The regain of secondary structure occurs with high efficiency even when little or no activity is recovered.
authors.affiliation: Department of Biological and Molecular Sciences, University of Stirling, Scotland, U.K.
authors.forename: S M
authors.initials: SM
authors.lastname: Kelly
authors.forename: N C
authors.initials: NC
authors.lastname: Price
mesh_terms: D000818:Animals; D002942:Circular Dichroism; D003956:Dialysis; D004229:Dithiothreitol / Q000494:pharmacology; D005649:Fumarate Hydratase / Q000737:chemistry*; D019791:Guanidine; D006146:Guanidines; D007700:Kinetics; D011487:Protein Conformation; D011489:Protein Denaturation; D013552:Swine
chemical_list: D006146:Guanidines; D005649:Fumarate Hydratase; D019791:Guanidine; D004229:Dithiothreitol