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The role of copper in the stability of ascorbate oxidase towards denaturing agents
I Savini1, S D'Alessio, A Giartosio
1Dipartimento di Medicina Sperimentale e Scienze Biochimiche, Università di Roma, Tor Vergata, Italy.
European Journal of Biochemistry
|July 5, 1990
Abstract:
The susceptibility of native, type-2 Cu-depleted and fully Cu-depleted ascorbate oxidase to thermal and chemical denaturation has been probed by differential scanning calorimetry, fluorimetry and circular dichroism. The data indicate that copper affects the stability, but not the protein conformation. The unfolding of ascorbate oxidase is characterized by a single endotherm. Calorimetric domains revealed by deconvolution are consistent with the domains identified by X-ray crystallography.