Reactivation of Immobilized Acetylcholinesterase-Tabun Complex by Methoxime and Its Homologues

Using an immobilized acetylcholinesterase-tabun enzyme-inhibitor complex, the reactivation efficacy of a homologous series of bispyridinium reactivators with increasing length of the alkylene chain between the pyridinium rings has been studied. The number of the alkylene groups in the chain ranged f...

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Bibliographic Details
Published in:Drug and chemical toxicology (New York, N.Y. 1978) N.Y. 1978), 2007-01, Vol.30 (2), p.97-103
Main Authors: Hoskovcová, Monika, Halámek, Emil, Kobliha, Zbyn k, Tušarová, Ivana
Format: Article
Language:English
Subjects:
Acetylcholinesterase
Acetylcholinesterase - drug effects
Acetylcholinesterase - metabolism
Animals
Biological and medical sciences
Bispyridinium aldoximes
Chemical and industrial products toxicology. Toxic occupational diseases
Chemical Warfare Agents - toxicity
Cholinesterase Inhibitors - toxicity
Cholinesterase Reactivators - pharmacology
Enzymes, Immobilized
Gas, fumes
Medical sciences
Methoxime
Organophosphates - toxicity
Oximes - pharmacology
Pyridinium Compounds - pharmacology
Reactivators
Structure-Activity Relationship
Swine
Tabun
Toxicology
Trimethoxime
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Summary:Using an immobilized acetylcholinesterase-tabun enzyme-inhibitor complex, the reactivation efficacy of a homologous series of bispyridinium reactivators with increasing length of the alkylene chain between the pyridinium rings has been studied. The number of the alkylene groups in the chain ranged from one to six. N,N′-Monomethylenebis(4-pyridiniumaldoxime) dibromide (MMB-4) and N,N′-trimethylenebis(4-pyridiniumaldoxime) dibromide (TMB-4) are the most efficient reactivators of the series.
ISSN:0148-0545
1525-6014
DOI:10.1080/01480540601186614