Abstract
Changes in the fluorescence of the reversibly bound dyes auramine O and 2,6-( p-toluidinyl)-naphthalenesulfonate and in the fluorescence of the intrinsic tryptophan were used to study the kinetics of acid denaturation of horse liver alcohol dehydrogenase. The fluorescence due to tryptophan and auramine O decrease during acid denaturation while the fluorescence due to the N-arylaminonaphthalene dye increases. Denaturation rates increase at higher ionic strength or lower pH. The results indicate that fluorescence probes have potential use in studies of protein denaturation.
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