Abstract
We report a pioneering analysis of the interaction between mammalian cholinesterases and 36 acylates and thioacylates of ammonium alcohols with different structure of an alkyl chain between ammonium and etheric atoms and with different structure of a cyclic ammonium group. Among these ethers, which were both substrates and reversible inhibitors of erythrocyte cholinesterase and serum butyrylcholinesterase, specific effectors of both enzymes were identified.
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