马拉硫磷对体外乙酰胆碱酯酶（EC 3.1.1.7）动力学参数的影响。
Effect of malathion on kinetic parameters of acetylcholinesterase (EC 3.1.1.7) in vitro.
作者信息
Kamal M A
机构信息
Department of Biochemistry, College of Science, King Saud University, Riyadh, Saudi Arabia.
出版信息
Biochem Mol Biol Int. 1997 Sep;43(1):89-97. doi: 10.1080/15216549700203851.
Kinetic analysis of the interaction of malathion with camel erythrocyte acetylcholinesterase was investigated in the present study. The Michaelis-Menten constant (K(m)) for the hydrolysis of acetylthiocholine iodide (ASCh) was found to be 53.15 microM and the Vmax was 0.287 mumol/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.
本研究对马拉硫磷与骆驼红细胞乙酰胆碱酯酶相互作用进行了动力学分析。发现碘化硫代乙酰胆碱（ASCh）水解的米氏常数（K(m)）为53.15微摩尔，最大反应速度（Vmax）为0.287微摩尔/分钟/毫克蛋白质。随着马拉硫磷浓度增加，表观米氏常数（Kmapp）和表观最大反应速度（Vmaxapp）均降低。狄克逊以及林-贝氏图及其二次重绘图表明，抑制类型为纯粹的非竞争性，抑制常数（Ki）值估计为102.1 ppm。随着ASCh浓度增加，表观抑制常数（Kiapp）降低，而表观最大抑制反应速度（Vmaxiapp）增加。
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