An analysis of sigmoid-shaped progress curves in the reaction between Elect
ric Eel acetylcholinesterase (acetylcholine aeetylhydrolase, EC 3.1.1.7, AC
hE) and its substrate acetylthiocholine in low concentrations at pH 7 is pr
esented. In order to be able to explain an initial apparent inhibition of t
he enzyme-substrate reaction, the rate of detection reaction had to be take
n into account. The theoretical curves obtained by the fitting of different
ial equations for the reaction mechanism to the data of six progress curves
simultaneously, exactly reproduce the course of the experimental curves. T
he measurements performed with various concentrations of detection reagent
confirm the proposed cause of sigmoidity.