Chemnitius J M, Dewald K, Kreuzer H, Zech R
Zentrum Innere Medizin, Georg-August-Universität, Göttingen, Germany.
Chem Biol Interact. 1993 Jun;87(1-3):239-44. doi: 10.1016/0009-2797(93)90048-4.
The kinetics of time- and concentration-dependent covalent organophosphorus inhibition of carboxylesterase isoenzymes (EC 3.1.1.1) and cholinesterase isoenzymes (EC 3.1.1.7 and EC 3.1.1.8) were investigated using a wide range of organophosphate inhibitor concentrations (10(-10)-10(-3) mol/l) and different inhibition times. Computerized analysis of inhibition curves by weighted non-linear least-squares curve fitting was compared to graphic analysis by iterative elimination of exponential functions. Possible experimental errors due to inhibitor saturation kinetics and enzymatic organophosphate hydrolysis were thoroughly investigated. In mammalian heart muscle, three different cholinesterase isoenzymes were identified. High sensitivity and specificity of the classic differential inhibition test for carboxylesterase activity of hen brain neuropathy target esterase (NTE) could be confirmed independently with both methods of inhibition curve analysis.
使用广泛的有机磷酸酯抑制剂浓度（10⁻¹⁰ - 10⁻³ mol/l）和不同的抑制时间，研究了时间和浓度依赖性共价有机磷对羧酸酯酶同工酶（EC 3.1.1.1）和胆碱酯酶同工酶（EC 3.1.1.7和EC 3.1.1.8）的抑制动力学。通过加权非线性最小二乘曲线拟合对抑制曲线进行计算机分析，并与通过指数函数的迭代消除进行的图形分析进行比较。对由于抑制剂饱和动力学和酶促有机磷酸酯水解导致的可能实验误差进行了全面研究。在哺乳动物心肌中，鉴定出三种不同的胆碱酯酶同工酶。两种抑制曲线分析方法均可独立证实经典差异抑制试验对母鸡脑神经病靶酯酶（NTE）羧酸酯酶活性具有高灵敏度和特异性。
