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Effect of malathion on kinetic parameters of acetylcholinesterase (EC 3.1.1.7)In vitro
Author(s) -
Kamal Mohammad Amjad
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700203851
Subject(s) - malathion , acetylthiocholine , acetylcholinesterase , chemistry , uncompetitive inhibitor , michaelis–menten kinetics , hydrolysis , enzyme , in vitro , iodide , aché , stereochemistry , chromatography , nuclear chemistry , medicinal chemistry , enzyme assay , biochemistry , non competitive inhibition , organic chemistry , pesticide , biology , agronomy
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.