Dealkylation and Loss of Capacity for Reactivation of Cholinesterase Inhibited by Sarin

Inhibition of rat brain acetylcholinesterase by $^{32}$P-sarin in vivo results initially in $^{32}$P-isopropylmethylphosphonylated enzyme. The percentage of inhibited enzyme that could not be reactivated by pyridinium aldoxime methochloride (aged enzyme) approximated the amount of radioactivity iden...

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Published inScience (American Association for the Advancement of Science) Vol. 154; no. 3747; pp. 404 - 407
Main Authors Harris, Larrel W., Fleisher, Joseph H., Clark, James, Cliff, William J.
Format Journal Article
LanguageEnglish
Published United States American Association for the Advancement of Science 21.10.1966
Subjects
Aging
Albumins
Animals
Brain Chemistry
Chemical suspensions
Cholinesterase inhibitors
Cholinesterase Inhibitors - pharmacology
Cholinesterases
Electrophoresis
Enzyme activity
Enzymes
Fractions
In Vitro Techniques
Oximes
Oximes - pharmacology
Pain
Phosphates - pharmacology
Radioactive decay
Radiometry
Rats
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Summary:Inhibition of rat brain acetylcholinesterase by $^{32}$P-sarin in vivo results initially in $^{32}$P-isopropylmethylphosphonylated enzyme. The percentage of inhibited enzyme that could not be reactivated by pyridinium aldoxime methochloride (aged enzyme) approximated the amount of radioactivity identified as $^{32}$P-methylphosphonate. The $^{32}$P-isopropyl methylphosphonate not released from the inhibited enzyme by the oxime accounted for 51 ± 10 percent (standard deviation) of the radioactivity fixed to brain tissue. It showed no correlation with aging and was probably bound to sites other than acetylcholinesterase.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0036-8075
1095-9203
DOI:10.1126/science.154.3747.404