| Title : Reactivation of immobilized acetylcholinesterase-tabun complex by pralidoxime, its isomers, and homologs - Hoskovcova_2010_Toxicol.Mech.Methods_20_223 |
| Author(s) : Hoskovcova M , Halamek E , Kobliha Z , Tusarova I |
| Ref : Toxicol Mech Methods , 20 :223 , 2010 |
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Abstract :
Reactivation efficacy of three homologous and three isomeric series of pralidoxime-type reactivators with aldoxime group in position 2, 3 and 4 of the heterocycle was tested in reactivation of tabun-inhibited AChE. The experiments were performed with immobilized and stabilized porcine brain AChE. The enzyme activity was measured by Ellman method. Reactivation efficacy was determined by measurement of indicator fabric coloration intensity as a measure of AChE activity. Of the studied group of nine reactivators, isomers with the functional group in position 2 were the most effective. The highest value (30 %) for reactivation of inhibited AChE was found for 2PAE after treatment for 15 min at concentration 0.5 mg/cm(3). The efficacy of the isomers decreased in the order ortho > para > meta. No marked effect on the efficacy of the reactivators was observed on prolongation of the reactivation time. The reactivators efficacy decreased with decreasing concentration of their solutions. |
| PubMedSearch : Hoskovcova_2010_Toxicol.Mech.Methods_20_223 |
| PubMedID: 20370537 |
Hoskovcova M, Halamek E, Kobliha Z, Tusarova I (2010)
Reactivation of immobilized acetylcholinesterase-tabun complex by pralidoxime, its isomers, and homologs
Toxicol Mech Methods
20 :223
Hoskovcova M, Halamek E, Kobliha Z, Tusarova I (2010)
Toxicol Mech Methods
20 :223