Author/Editor     Arsov, Zoran; Zorko, Matjaž; Schara, Milan
Title     Inhibition of erythrocyte acetylcholinesterase by n-butanol at high concentrations
Type     članek
Source     Arch Biochem Biophys
Vol. and No.     Letnik 437
Publication year     2005
Volume     str. 78-84
ISSN     0003-9861
Language     eng
Abstract     Erythrocyte acetylcholinesterase (AChE) is bound to the membrane by a complex glycosylphosphatidylinositol anchor, so the effect of alcohol on AChE activity may reflect direct and/or membrane-mediated effects. The indication of a direct interaction between n-butanol and AChE molecules is the activation/inhibition of AChE by occupation of the enzyme's active and/or regulatory sites by alcohol. The activation of AChE can occur only at low concentrations of alcohols, while at high concentrations AChE is inhibited. In this work the mechanism of inhibition of erythrocyte AChE by n-butanol at high concentrations was studied. The values of activity, calculated assuming parabolic competitive inhibition, which implies that one or two molecules of inhibitor bind to the enzyme, fit well to the experimental values. From the values of the inhibition constants it was concluded that al high n-butanol concentrations two alcohol molecules usually interact with AChE.
Descriptors     ERYTHROCYTE MEMBRANE
MEMBRANE PROTEINS
ACETYLCHOLINESTERASE
ALCOHOLS, BUTYL
GLYCOSYLPHOSPHATIDYLINOSITOLS
CATTLE
TEMPERATURE
ALCOHOL, ETHYL