title: Increased catalytic activity of protein disulfide isomerase using aromatic thiol based redox buffers.
abstract: PDI is an enzyme that acts as a chaperone, shufflase, and oxidase during the folding of disulfide-containing proteins. The ability of aromatic thiols to increase the activity of PDI-catalyzed protein folding over that of the standard thiol glutathione (GSH) was measured. 4-Mercaptobenzoic acid (ArSH) increased the activity of PDI by a factor of three.
authors.affiliation: Department of Chemistry, Syracuse University, Syracuse, NY 13244, USA.
authors.forename: Jonathan D
authors.initials: JD
authors.lastname: Gough
authors.forename: Watson J
authors.initials: WJ
authors.lastname: Lees
mesh_terms: D002021:Buffers; D002384:Catalysis / Q000187:drug effects; D006801:Humans; D007700:Kinetics; D010084:Oxidation-Reduction; D019704:Protein Disulfide-Isomerases / Q000737:chemistry / Q000378:metabolism*; D017510:Protein Folding; D012259:Ribonuclease, Pancreatic / Q000737:chemistry; D013329:Structure-Activity Relationship; D013438:Sulfhydryl Compounds / Q000494:pharmacology*
chemical_list: D002021:Buffers; D013438:Sulfhydryl Compounds; D012259:Ribonuclease, Pancreatic; D019704:Protein Disulfide-Isomerases