In vitro studies on the reactivation by oximes of phosphylated acetylcholinesterase--I. On the reactions of P2S with various organophosphates and the properties of the resultant phosphylated oximes

Biochem Pharmacol. 1986 Mar 1;35(5):737-44. doi: 10.1016/0006-2952(86)90240-6.

Abstract

The rates of formation and decomposition of a series of phosphylated oximes derived from P2S (2-hydroxy-iminomethyl-1-methylpyridinium methane-sulphonate) have been measured. The rates of inhibition of AChE by these phosphylated oximes and the parent (and related) organophosphates have also been measured. Possession of these rate data now permits a detailed analysis of the reactivation of phosphylated AChE by P2S to be made (see following paper).

MeSH terms

  • Acetylcholinesterase*
  • Animals
  • Cattle
  • Chemical Phenomena
  • Chemistry
  • Cholinesterase Inhibitors / antagonists & inhibitors*
  • Cholinesterase Reactivators*
  • Kinetics
  • Organophosphorus Compounds / antagonists & inhibitors*
  • Oximes*
  • Water

Substances

  • Cholinesterase Inhibitors
  • Cholinesterase Reactivators
  • Organophosphorus Compounds
  • Oximes
  • Water
  • Acetylcholinesterase