Neurobiology of Acetylcholine

Kinetic analysis of the interaction of malathion with camel erythrocyte acetylcholinesterase was investigated in the present study. The Michaelis‐Menten constant (Km) for the hydrolysis of acetylthiocholine iodide (ASCh) was found to be 53.15 μM and the Vmax was 0.287 μmol/min/mg protein. The Kmapp and Vmaxapp were both decreased by increased malathion concentration. Dixon as well as Lineweaver‐Burk plots and their secondary replots indicated that the nature of the inhibition was of the pure uncompetitive type with Ki value estimated as 102.1 ppm. The Kiapp decreased while Vmaxiapp increased by an increased concentration in ASCh.

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Neurobiology of Acetylcholine

Cited by 4 publications

References 386 publications

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Effect of malathion on kinetic parameters of acetylcholinesterase (EC 3.1.1.7)In vitro

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