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Spontaneously reactivation of acetylcholinesterase inhibited by diisopropylfluorophosphate.
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Kinetic analysis of species difference in acetylcholinesterase sensitivity to organophosphate insecticides.
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Determination of the rate constant of enzyme modification by measuring the substrate reaction in the presence of the modifier.
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A theoretical kinetic analysis of the protective action exerted by eserine and other carbamate anticholinesterases against poisoning by organophosphorus compounds.
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Kinetics for the inhibition of acetylcholinesterase from the electric eel by some organophosphates and carbamates.
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Acceleration by free carbamate of the spontaneous reactivation of carbamylated acetylcholinesterase.
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Recording spectrophotometric method for determination of dissociation and phosphorylation constants for the inhibition of acetylcholinesterase by organophosphates in the presence of substrate.
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Carbamylated acetylcholinesterase: acceleration of decarbamylation by bispyridinium oximes.
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Determination of rate constants for the irreversible inhibition of acetylcholine esterase by continuously monitoring the substrate reaction in the presence of the inhibitor.
Biochim Biophys Acta. 1986 Mar 28;870(2):185-90. doi: 10.1016/0167-4838(86)90220-7.
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On the difficulties of fitting the double Michaelis-Menten equation to kinetic data.
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