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., Martorana, G., Meucci Calabrese, E., Santini, S. A., Castelli, A., Alkaline phosphatase inactivation by mixed function oxidation systems, <<ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS>>, 1987; 258 (1): 176-185. [doi:10.1016/0003-9861(87)90334-1] [http://hdl.handle.net/10807/9391]
Alkaline phosphatase inactivation by mixed function oxidation systems
Mordente, Alvaro;Meucci Calabrese, 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.
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