肟诱导被氨基磷酸酯抑制的乙酰胆碱酯酶重新激活。
Oxime-induced reactivation of acetylcholinesterase inhibited by phosphoramidates.
作者信息
Jokanović M, Maksimović M, Kilibarda V, Jovanović D, Savić D
机构信息
Faculty of Pharmacy, Department of Toxicology, Belgrade, Yugoslavia.
出版信息
Toxicol Lett. 1996 Apr;85(1):35-9. doi: 10.1016/0378-4274(96)03634-x.
The reaction of human erythrocyte acetylcholinesterase (AChE) with a set of structurally related phosphoramidates was studied in order to investigate the properties of phosphorylated enzyme and the effects of 4 oximes PAM-2, TMB-4, HI-6 and BDB-106 on the reactivation of inhibited AChE. Second-order rate constant of the phosphorylation reaction of the compounds towards the active site of AChE range between 5.0 x 10(2) and 4.9 x 10(6) M-1min-1 and their inhibitory power (I50) was from 7.3 x 10(-5) to 5.7 x 10(-9) M for 20 min incubation at 37 degrees C. The oximes used were weak reactivators of inhibited AChE except for (C4H9O)(NH2)P(O)DCP (DCP, -O-2,5-dichlorphenyl group) and (C6H13O)(NH2)P(O)SCH3 where we have obtained good reactivation. Imidazole oxime BDB-106 proved to be a potent reactivator of tabun-inhibited AChE.
为了研究磷酸化酶的性质以及4种肟类化合物PAM - 2、TMB - 4、HI - 6和BDB - 106对被抑制的乙酰胆碱酯酶（AChE）再活化的影响，研究了人红细胞乙酰胆碱酯酶（AChE）与一组结构相关的氨基磷酸酯的反应。这些化合物与AChE活性位点的磷酸化反应的二级速率常数在5.0×10²至4.9×10⁶ M⁻¹min⁻¹之间，在37℃孵育20分钟时，它们的抑制能力（I50）为7.3×10⁻⁵至5.7×10⁻⁹ M。除了（C₄H₉O）（NH₂）P（O）DCP（DCP，-O-2,5-二氯苯基）和（C₆H₁₃O）（NH₂）P（O）SCH₃（在这两种化合物中我们获得了良好的再活化效果）外，所使用的肟类化合物是被抑制的AChE的弱再活化剂。咪唑肟BDB - 106被证明是塔崩抑制的AChE的有效再活化剂。
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