Anaerobic treatment with cyanide of reduced ascorbate oxidase causes total depletion of copper. No significant amount of the metal is reincorporated when the apo-enzyme is incubated with cupric ions, but it is upon incubation with a stoichiometric amount (8 mol per mol of native enzyme) of a Cu(I) complex stable in air [Cu(I)(thiourea)3]Cl. The yield in reconstituted protein is higher under anaerobic conditions (85-90%) than in air (70-75%). By treatment with less than stoichiometric amounts of [Cu(I)(thiourea)3]Cl the apo-protein binds copper preferentially at the blue copper site. As a consequence the recovery of enzymatic activity is percentually lower than copper reincorporation.
Savini I., M.L. (1985). Full, reversible copper removal from ascorbate oxidase. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 131(3), 1251-1255.
Tipologia: | Articolo su rivista |
Citazione: | Savini I., M.L. (1985). Full, reversible copper removal from ascorbate oxidase. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 131(3), 1251-1255. |
IF: | Con Impact Factor ISI |
Lingua: | English |
Settore Scientifico Disciplinare: | Settore BIO/10 |
Revisione (peer review): | Sì, ma tipo non specificato |
Tipo: | Articolo |
Rilevanza: | Rilevanza internazionale |
Stato di pubblicazione: | Pubblicato |
Data di pubblicazione: | 1985 |
Titolo: | Full, reversible copper removal from ascorbate oxidase |
Autori: | |
Autori: | Savini I., Morpurgo L., Avigliano L. |
Appare nelle tipologie: | 01 - Articolo su rivista |