Alkaline phosphatase is inactivated by mixed function oxidation systems. OH. radicals, generated via an ascorbate-modified Haber-Weiss cycle or a Fenton-type reaction, seem to be responsible for the protein oxidative damage. Experiments with hydroxyl radical scavengers, enzyme substrates, products, and metal cofactors suggest that a "site-specific" radical attack takes place at or near the active center. Vitamin E fails to protect alkaline phosphatase; uric acid, instead, is particularly effective in shielding the protein against covalent modifications.

Mordente, A., Miggiano, G. A. D., Martorana, G. E., Meucci, E., Santini, S. A., Castelli, A., Alkaline phosphatase inactivation by mixed function oxidation systems, <<ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS>>, N/A; 258 (1): 176-185 [http://hdl.handle.net/10807/37271]

Alkaline phosphatase inactivation by mixed function oxidation systems

Mordente, Alvaro;Miggiano, Giacinto Abele Donato;Martorana, Giuseppe Ettore;Meucci, Elisabetta;Santini, Stefano Angelo;
1987

Abstract

Alkaline phosphatase is inactivated by mixed function oxidation systems. OH. radicals, generated via an ascorbate-modified Haber-Weiss cycle or a Fenton-type reaction, seem to be responsible for the protein oxidative damage. Experiments with hydroxyl radical scavengers, enzyme substrates, products, and metal cofactors suggest that a "site-specific" radical attack takes place at or near the active center. Vitamin E fails to protect alkaline phosphatase; uric acid, instead, is particularly effective in shielding the protein against covalent modifications.
Inglese
Mordente, A., Miggiano, G. A. D., Martorana, G. E., Meucci, E., Santini, S. A., Castelli, A., Alkaline phosphatase inactivation by mixed function oxidation systems, <>, N/A; 258 (1): 176-185 [http://hdl.handle.net/10807/37271]
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/10807/37271
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