Prozorovskii_1996_Biokhimiia_61_690

The properties of aminostigmine in comparison with those of other carbamate inhibitors of cholinesterases have been studied in vitro using potentiometric titration and Ellman methods. The bimolecular constants of the inhibition rate of acetyl-, butyryl- and propionylcholinesterase were found to be equal to (8.0-14.0).10(5) (3.8-7.7).10(5) and 11.0.10(5) M-1.min-1, respectively. In terms of inhibitory activity, aminostrigmine is comparable to neostigmine methylsulphate, being inferior to physostigmine and superior to pyridistigmine. The rate of decarbamylation of acetylcholinesterase inhibited by aminostigmine measured by the dilution method, by creating excessive acetylcholine and by dialysis is characterized by k2c constants equal to (1.1-1.6).10(-2), (2.5-2.8).10(-2) and 0.025.10(-2) min-1, respectively. On the whole, aminostigmine belongs to slowly reversible inhibitors. Being carbamylated by aminostigmine, the enzyme is resistant to reactivation by TMB-4(Trimedoxime) and HI-6. At (4-6).10(-7) M aminostigmine prevents by 50% the irreversible binding of cholinesterase by certain organophosphate inhibitors of cholinesterase when the latter are used at concentrations needed to inhibit the enzymatic activity by 85-90%.