Ascorbic acid, isoascorbic acid and dehydroascorbic acid inhibit bovine kidney alkaline phosphatase activity. Ascorbic acid free radicals seem not to be involved. Dialysis does not make the inactivation reversible. A competitive mechanism can be inferred from experiments with phosphate and substrates, which block the activity decay. The influence of temperature, pH, other inhibitors and tertiary structure modifications on the inactivation process is also investigated.

Miggiano, G., Mordente, A., Martorana, G., Meucci Calabrese, E., Castelli, A., Characterization of alkaline phosphatase inactivation by ascorbic acid, <<BIOCHIMICA ET BIOPHYSICA ACTA>>, 1984; 789 (3): 343-346. [doi:10.1016/0167-4838(84)90190-0] [http://hdl.handle.net/10807/9864]

Characterization of alkaline phosphatase inactivation by ascorbic acid

Miggiano, Ga;Mordente, Alvaro;Meucci Calabrese, Elisabetta;
1984

Abstract

Ascorbic acid, isoascorbic acid and dehydroascorbic acid inhibit bovine kidney alkaline phosphatase activity. Ascorbic acid free radicals seem not to be involved. Dialysis does not make the inactivation reversible. A competitive mechanism can be inferred from experiments with phosphate and substrates, which block the activity decay. The influence of temperature, pH, other inhibitors and tertiary structure modifications on the inactivation process is also investigated.
1984
Inglese
Inglese
Miggiano, G., Mordente, A., Martorana, G., Meucci Calabrese, E., Castelli, A., Characterization of alkaline phosphatase inactivation by ascorbic acid, <<BIOCHIMICA ET BIOPHYSICA ACTA>>, 1984; 789 (3): 343-346. [doi:10.1016/0167-4838(84)90190-0] [http://hdl.handle.net/10807/9864]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10807/9864
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