Abstract
Acetylcholinesterase (Acetylcholine acetylhydrolase E.C. 3.1.1.7.) released from a rat brain synaptosomal fraction was shown to rebind upon incubation in the presence of 3 mM acetylcholine. This action was shown to be reversible. Glutamate, aspartate and gamma-aminobutyrate antagonise this effect. Solubilization of both bulk protein and acetylcholinesterase by Lubrol WX and triton X 100 after acetylcholine incubation of synaptosomal fractions is much lower than in the non incubated preparation. Local production of protons due to the hydrolysis of acetylcholine by the enzyme could partially explain the reassociation of the enzyme. We suggest that the observed phenomenon may play some physiological role in the function of acetylcholinesterase.
Published Version
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