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Investigating the kinetics of paramagnetic-beads linked alkaline phosphatase enzyme through microchannel resistance
Mathilde Faure1, Bruno Sotta2, Jean Gamby1
1CNRS, UMR 8235, LISE, F-75005 Paris, France; Sorbonne Universités, UPMC Univ Paris 06, UMR 8235, Laboratoire Interfaces et Systèmes Electrochimiques, F-75005 Paris, France.
Abstract:
Real time monitoring of electrolyte resistance changes during hydrolysis of 4-nitrophenylphosphate (pNPP) by alkaline phosphatase (ALP) bound on paramagnetic-beads was performed into a small dielectric channel. The reaction kinetic fit with a non-competitive substrate-inhibition equation. Michaelis-Menten apparent constant, KM(app), was determined as 0.33±0.06mM and the maximum apparent rate, Vmax(app) as 98±5pMs(-1). The detection limits were 15fM for ALP and 0.75mM for pNPP. This miniaturized device constitutes a powerful tool for analysis of interaction between ligands.
