Brestkin_1991_Ukr.Biokhim.Zh_63_51

The reversible inhibition of horse blood serum butyrylcholinesterase (Ce 3.1.1.8) hydrolysis of ion substrates of acetyl- and butyrylthiocholines and non-ion substrate of indophenylacetate by N-methyl-4-piperidinylbenzylate and tacrine (1,2,3,4,-tetrahydro-9-aminoacridine) and phosphate buffer and ethanol influence on this process are investigated. The values of competitive Ki, uncompetitive K'i and generalized K sigma inhibitory constants are determined. It is shown that the inhibition effect and reversible inhibition type depend not only on the inhibitor and substrate nature but also on the phosphate buffer concentration and ethanol presence in the reaction mixture.