The binding of sarin in the blood plasma of the rat
article
Sephadex filtration of serum from rats 10 min after injection of 50 μg/kg of 32P-sarin demonstrated that about 70 per cent of the radioactivity present in the serum was attached to molecules with a molecular weight above 10,000. Incubation of samples of this serum with oximes caused a decrease in the amounts of 32P attached to the large molecules and an increase in those appearing in the micromolecular fractions. The oximes apparently released 32P from the large molecules. DAM and MINA were much more effective in this respect than P-2-AM and TMB-4. The activities of the ChE and AE in serum from rats 10 min after injection of sarin were determined. Both enzymes were partly inactivated. The AE reactivating potencies of the oximes concurred with their 32P releasing effects: DAM and MINA (0.5 mM) partly reactivated the AE, but P-2-AM and TMB-4 did not. In contrast TMB-4, P-2-AM and MINA produced a partial reactivation of the ChE whereas DAM had no effect. It was concluded that the obtained results support the idea that the large molecules in the serum to which the radioactivity was attached were identical with AE. © 1970.
Topics
AcetylcholinesteraseCholinesteraseCholinesterase inhibitorOximePhosphonic acid derivativePhosphorusPralidoximeAnimalBloodDrug effectEnzyme activationFemaleGel chromatographyIntraperitoneal drug administrationIntravenous drug administrationMacromoleculeMetabolismMolecular weightProtein bindingRatChromatography, GelEnzyme ActivationInjections, IntraperitonealInjections, IntravenousMacromolecular SystemsMolecular WeightPhosphonic AcidsPhosphorus IsotopesPralidoxime CompoundsProtein Binding
TNO Identifier
227160
ISSN
00062952
Source
Biochemical Pharmacology, 19(3), pp. 877-881.
Pages
877-881
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