Arsov_2005_Arch.Biochem.Biophys_437_78

Reference

Title : Inhibition of erythrocyte acetylcholinesterase by n-butanol at high concentrations - Arsov_2005_Arch.Biochem.Biophys_437_78
Author(s) : Arsov Z , Zorko M , Schara M
Ref : Archives of Biochemistry & Biophysics , 437 :78 , 2005
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 at high n-butanol concentrations two alcohol molecules usually interact with AChE.

PubMedSearch : Arsov_2005_Arch.Biochem.Biophys_437_78
PubMedID: 15820219

Related information

Citations formats

Arsov Z, Zorko M, Schara M (2005)
Inhibition of erythrocyte acetylcholinesterase by n-butanol at high concentrations
Archives of Biochemistry & Biophysics 437 :78

Arsov Z, Zorko M, Schara M (2005)
Archives of Biochemistry & Biophysics 437 :78