Influence of Temperature and Cholinergic Ligands on the Carbamylation of Unmodified and Carbodiimide-Modified Erythrocyte Acetylcholinesterase,
BRITISH COLUMBIA UNIV VANCOUVER FACULTY OF PHARMACEUTICAL SCIENCES
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It is shown that only the neuromuscular blocking agents accelerate carbamylation of the esteratic site of the enzyme by a neutral carbamate, whereas inorganic ions have no effect and small quaternary ammonium compounds inhibit this reaction. All of the ligands examined inhibited carbamylation by neostigmine. The authors have demonstrated that the same allosteric site that functions in the acceleration of deacetylation of the enzyme also functions in acceleration of carbamylation. The influence of temperature on the ligand-induced activation and inhibition of the carbamylation was studied in the hope of gaining further information on the related mechanisms occurring at the cholinergic receptor.