The role of copper in the stability of ascorbate oxidase towards denaturing agents.


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. Study holds ProTherm entries: 7569, 7570, 7571, 7572, 7573, 7574 Extra Details: susceptibility; Cu-depleted ascorbate oxidase;,protein conformation; endotherm; deconvolution

Submission Details

ID: nDbz6y934

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:34 p.m.

Version: 1

Publication Details
Savini I;D'Alessio S;Giartosio A;Morpurgo L;Avigliano L,Eur. J. Biochem. (1990) The role of copper in the stability of ascorbate oxidase towards denaturing agents. PMID:2373076
Additional Information

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