Reagent-less detection of a competitive inhibitor of immobilized acetylcholinesterase.
The interaction of monosulfonate tetraphenyl porphine (TPPS(1)) with immobilized acetylcholinesterase (AChE) yields a characteristic absorbance peak at 446 nm. Addition of acetylcholine iodide or the competitive inhibitor tetracaine to the immobilized TPPS(1)-AChE complex results in a decrease in absorbance intensity at 446 nm due to displacement of the porphyrin from the active site. The loss in intensity at 446 nm is linearly dependent on tetracaine concentration at levels below 100 ppb. Tetracaine concentrations as low as 300 ppt have been detected.
White
Brandy J
BJ
Department of Physics, Oklahoma State University, Stillwater, OK 74078, USA.
Legako
J Andrew
JA
Harmon
H James
HJ
D000110:Acetylcholinesterase / Q000378:metabolism*; D000818:Animals; D001667:Binding, Competitive; D015374:Biosensing Techniques; D002800:Cholinesterase Inhibitors / Q000032:analysis* / Q000494:pharmacology; D004593:Electrophorus; D004800:Enzymes, Immobilized; D066298:In Vitro Techniques; D011166:Porphyrins / Q000378:metabolism; D013053:Spectrophotometry; D013748:Tetracaine / Q000032:analysis / Q000494:pharmacology
D002800:Cholinesterase Inhibitors; D004800:Enzymes, Immobilized; D011166:Porphyrins; D013748:Tetracaine; C016136:tetraphenylporphine sulfonate; D000110:Acetylcholinesterase