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.
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