The enzyme, yeast alcohol dehydrogenase, was examined by differential scanning calorimetry and fluorescence spectroscopy. As indicated by the magnitude of the temperature at which the heat effect due to unfolding is maximal, and the temperature range over which unfolding occurs, the yeast enzyme appears to be less stable than its horse liver counterpart. Additionally, altering the pH from 6.0 appears destabilize the enzyme. The spectral shift in maximal emission wavelength that accompanies an alteration in pH suggests that structural changes occur at extreme values of acid and alkaline pH. When slow scan rate experiments were performed, two separate heat effects could be resolved. The results of our and prior fractionation work indicate that the two heat effects are likely due to two molecular species, and not domains within the YADH molecule.
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