Abstract
Long before acetylcholine (ACh) was recognized to be a transmitter substance, the presence in the blood of an enzyme capable of degrading ACh had been postulated by Sir Henry Dale.1 The existence of such an esterase hydrolyzing ACh was demonstrated in blood plasma by Staedman and co-workers in 1932.2 Extensive studies during the following years contributed information on different types of cholinesterases (ChEs), their kinetic properties, and distribution in excitable tissues. During World War II, it was recognized that the inhibition of ChE was the basis for the high toxicity of organophosphates,3 which could be used as insecticides and also as potential chemical warfare agents. Soon after, the theoretical grounds were laid for the design of the nucleophilic agents that proved to be efficient reactivators of AChE inhibited by organophosphate agents.4–6
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Brzin, M., Sketelj, J., Klinar, B. (1983). Cholinesterases. In: Lajtha, A. (eds) Handbook of Neurochemistry. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1881-9_11
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