Abstract
The thermal unfolding of glutathione synthetase was studied in three different buffers at pH 7.5 by differential scanning calorimetry. Variation of protein concentration caused the change in the peak temperature of DSC curves observed. It was found that the calorimetric enthalpy becomes larger as the buffer ionization heat becomes larger. The results were discussed in the terms of a possible involvement of the process characterized by a dissociation of the terameric enzyme into monomeric unit during the unfolding.
