title: Analysis of cholinesterase binding to a carnitine-modified EQCM sensor.
abstract: A sensor for cholinesterases (ChEs) has been developed by binding carnitine via 1,6-diaminohexane to a mixed monolayer of 11-mercaptoundecanoic acid/11-mercapto-1-undecanol on the surface of a gold-coated quartz crystal. Catalytically active and organophosphate-inhibited acetyl- and butyryl-cholinesterases of different origins were tested for their binding ability to D- and L-carnitine, respectively. The binding constants were calculated by using a one-to-one binding model. Additionally, the activity of the immobilized ChE was monitored and the operational stability was investigated amperometrically.
authors.affiliation: Department of Analytical Biochemistry, Institute of Biochemistry and Biology, University of Potsdam, Karl-Liebknecht-Strasse 24-25, 14476 Golm, Germany. zeravik@uni-potsdam.de
authors.forename: Jiri
authors.initials: J
authors.lastname: Zeravik
authors.forename: Carsten
authors.initials: C
authors.lastname: Teller
authors.forename: Frieder W
authors.initials: FW
authors.lastname: Scheller
mesh_terms: D000818:Animals; D015374:Biosensing Techniques; D002331:Carnitine; D002802:Cholinesterases / Q000032:analysis*; D004331:Drosophila melanogaster / Q000201:enzymology
chemical_list: D002802:Cholinesterases; D002331:Carnitine