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The inhibition of acetylcholinesterase by arsenite and fluoride

Authors
Journal
Archives of Biochemistry and Biophysics
0003-9861
Publisher
Elsevier
Publication Date
Volume
226
Issue
2
Identifiers
DOI: 10.1016/0003-9861(83)90318-1
Keywords
  • Enzyme Mechanisms And Metabolism
Disciplines
  • Biology

Abstract

Abstract The effect of fluoride on the rate of reaction of acetylcholinesterase with arsenite, on the rate of dissociation of the enzyme-arsenite complex, and on the equilibrium between enzyme and arsenite was studied. Fluoride decreases the rate of the reaction between acetylcholinesterase and arsenite and changes the apparent equilibrium dissociation constant between the enzyme and arsenite, but even at concentrations as high as 0.2 m has no effect on the rate of dissociation of the enzyme-arsenite complex. The binding of fluoride and arsenite with the enzyme is highly anticooperative and may well be mutually exclusive. These results are consistent with a model in which the binding sites overlap and in which the same functional groups are involved.

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