TY - JOUR
T1 - Characterization of alkaline phosphatase inactivation by ascorbic acid
AU - Miggiano, Giacinto Abele Donato
AU - Mordente, Alvaro
AU - Martorana, Giuseppe E.
AU - Meucci Calabrese, Elisabetta
AU - Castelli, Adriano
PY - 1984
Y1 - 1984
N2 - 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.
AB - 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.
KW - Alkaline Phosphatase
KW - Animals
KW - Ascorbic Acid
KW - Binding, Competitive
KW - Cattle
KW - Dehydroascorbic Acid
KW - Hydrogen-Ion Concentration
KW - Kidney
KW - Structure-Activity Relationship
KW - Temperature
KW - Alkaline Phosphatase
KW - Animals
KW - Ascorbic Acid
KW - Binding, Competitive
KW - Cattle
KW - Dehydroascorbic Acid
KW - Hydrogen-Ion Concentration
KW - Kidney
KW - Structure-Activity Relationship
KW - Temperature
UR - http://hdl.handle.net/10807/9864
U2 - 10.1016/0167-4838(84)90190-0
DO - 10.1016/0167-4838(84)90190-0
M3 - Article
SN - 0006-3002
VL - 789
SP - 343
EP - 346
JO - BIOCHIMICA ET BIOPHYSICA ACTA
JF - BIOCHIMICA ET BIOPHYSICA ACTA
ER -