Abstract
The review is devoted to studies on the combined inhibition of the catalytic activity of cholinesterases by organophosphorus compounds. This type of inhibition depends significantly on the presence of hydrophobic substituents in the organophosphorus molecule. It is suggested that there is a possibility of "concerted" or "non-concerted" sorption of the hydrophobic groups of the inhibitor on the hydrophobic regions in the vicinity of the anionic and esterase sites on the active surfaces of cholinesterases. These effects apparently determine the nature of the inhibition of cholinesterases.
The bibliography includes 44 references.