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. 1977 Aug 11;483(2):312-9.
doi: 10.1016/0005-2744(77)90059-6.

Spontaneous reactivation of acetylcholinesterase following organophosphate inhibition. I. An analysis of anomalous reactivation kinetics

J W Hovanec, C A Broomfield, G M Steinberg, K W Lanks, C N Lieske

Spontaneous reactivation of acetylcholinesterase following organophosphate inhibition. I. An analysis of anomalous reactivation kinetics

J W Hovanec et al. Biochim Biophys Acta. .

Abstract

The first kinetic studies on the spontaneous reactivation of Sarin-inhibited acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) are reported. With increasing pH the extent of reactivation increases while the observed rate constant decreases. An analysis of the change in aging rate constant as a function of pH suggests that the aging of alkyl-alkoxy phosphonylated acetylcholinesterases is not solely acid catalyzed.

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