Kinetic behaviour of acetylcholinesterase from muscle microsomal membranes.

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Munoz-Delgado E, Vidal CJ

Kinetic behaviour of acetylcholinesterase from muscle microsomal membranes.

Biochem Int. 1986 Oct;13(4):625-32.

PubMed ID

3801037 [ View in PubMed

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Abstract

In order to determine whether catalytic hydrolysis of acetylcholine, observed in muscle microsomes enriched in sarcoplasmic reticulum membranes, was carried out by true acetylcholinesterase we studied the substrate specificity of this enzyme, its kinetic behaviour and its sensitivity against several reversible inhibitors. The results showed that the enzyme from muscle microsomes had acetylcholine (or acetylthiocholine) as the preferent substrate and was also able to hydrolyze acetyl-beta-methylcholine. The enzyme had a Km of 100-120 microM, being inhibited by a high substrate concentration. Acetylcholinesterase in this source was competitively inhibited by BW-284-c-51, eserine and decamethonium with ki values of 0.025 microM, 0.021 microM and 65 microM, respectively. The enzyme was poorly inhibited by the pseudocholinesterase inhibitor ethopropazine. The results show that the hydrolytic enzyme is indeed acetylcholinesterase.

DrugBank Data that Cites this Article

Drug Enzymes

Drug	Enzyme	Kind	Organism	Pharmacological Action	Actions
Decamethonium	Cholinesterase	Protein	Humans	Unknown	Inhibitor	Details