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使用肟K027在体外对乙酰胆碱酯酶进行再激活。

In vitro reactivation of acetylcholinesterase using the oxime K027.

作者信息

Kuca Kamil, Kassa Jirí

机构信息

Purkyne Military Medical Academy, Department of Toxicology, PO Box 35/T, 500 01 Hradec Králové, Czech Republic.

出版信息

Vet Hum Toxicol. 2004 Feb;46(1):15-8.

Abstract

The ability of a new bisquaternary oxime, K027 (1-[4-hydroxyiminomethylpyridinium]-3-[carbamoylpyridinium] propane dibromide), to reactivate the enzyme acetylcholinesterase (AChE) inhibited by the nerve agents Tabun, sarin and VX was evaluated. Its reactivation potency was compared to the AChE reactivators pralidoxime (2-PAM), obidoxime and HI-6; K027 seems a good reactivator of organophosphates-inhibited AChE. Its reactivation potency is lower compared to the other oximes for reactivation of sarin-inhibited AChE, but it is sufficient to significantly increase the activity of sarin-inhibited AChE. Its reactivation ability is comparable to obidoxime for reactivation of VX- and tabun-inhibited AChE and is higher than the reactivation potency of HI-6, for tabun-inhibited AChE. HI-6 is currently regarded the most promising reactivator of organophosphates-inhibited AChE.

摘要

对一种新型双季铵肟K027(1-[4-羟基亚胺甲基吡啶鎓]-3-[氨基甲酰基吡啶鎓]丙烷二溴化物)使被神经毒剂塔崩、沙林和维埃克斯抑制的乙酰胆碱酯酶(AChE)重新活化的能力进行了评估。将其重新活化效力与AChE重新活化剂氯解磷定(2-PAM)、双复磷和HI-6进行了比较;K027似乎是有机磷酸酯抑制的AChE的良好重新活化剂。在重新活化沙林抑制的AChE方面,其重新活化效力低于其他肟类,但足以显著提高沙林抑制的AChE的活性。在重新活化维埃克斯和塔崩抑制的AChE方面,其重新活化能力与双复磷相当,在重新活化塔崩抑制的AChE方面,其重新活化效力高于HI-6。HI-6目前被认为是有机磷酸酯抑制的AChE最有前景的重新活化剂。

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