L-ascorbic acid preincubation with rabbit kidney (Na+-K+)-ATPase inhibits the activity of p-nitrophenylphosphatase partial reaction with a pseudo-first order decay. The presence of the pseudosubstrate, p-nitrophenylphosphate, counteracts the inhibiting effect. During the reaction course, the kinetic rate is enhanced at ascorbic acid concentrations below 0.7 mmol/1, but is inhibited above that amount. The intrinsic fluorescence of the enzyme in E1 and E2 conformations is modified suggesting the occurrence of ascorbate-induced intermediate forms, distinct from those provoked by the addition of cations, magnesium and phosphate. These destabilized forms appear easier to be converted into catalytically active or increasingly inhibited states.
Miggiano, G. A. D., Martorana, G., Mordente, A., Di Bonifacio, L., Castelli, A., (Na+-K+)-ATPase interaction with L-ascorbic acid. Effect on p-nitrohenylphosphatase partial reaction, <<ITALIAN JOURNAL OF BIOCHEMISTRY>>, 1989; 37 (5): 284-292 [http://hdl.handle.net/10807/9696]
(Na+-K+)-ATPase interaction with L-ascorbic acid. Effect on p-nitrohenylphosphatase partial reaction
Miggiano, Giacinto Abele Donato;Mordente, Alvaro;
1988
Abstract
L-ascorbic acid preincubation with rabbit kidney (Na+-K+)-ATPase inhibits the activity of p-nitrophenylphosphatase partial reaction with a pseudo-first order decay. The presence of the pseudosubstrate, p-nitrophenylphosphate, counteracts the inhibiting effect. During the reaction course, the kinetic rate is enhanced at ascorbic acid concentrations below 0.7 mmol/1, but is inhibited above that amount. The intrinsic fluorescence of the enzyme in E1 and E2 conformations is modified suggesting the occurrence of ascorbate-induced intermediate forms, distinct from those provoked by the addition of cations, magnesium and phosphate. These destabilized forms appear easier to be converted into catalytically active or increasingly inhibited states.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.