Yeast glyoxalase I. Circular dichroic spectra and pH effects.

Large scale isolation and physicochemical characterisation of yeast glyoxalase I showed that this enzyme contained small amounts of carbohydrates. Circular dichroic spectra of the enzyme measured in the presence and absence of S-(p-bromobenzyl)glutathione indicated perturbation of a tyrosine on binding of this competitive inhibitor. Values of Ki for competitive inhibitors were pH invariant over the accessible pH range.