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Pretreatment with pyridinium oximes improves antidotal therapy against tabun poisoning (CROSBI ID 125388)

Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija

Lucić Vrdoljak, Ana ; Čalić, Maja ; Radić, Božica ; Berend, Suzana ; Jun, Daniel ; Kuča, Kamil ; Kovarik, Zrinka Pretreatment with pyridinium oximes improves antidotal therapy against tabun poisoning // Toxicology, 228 (2006), 41-50-x

Podaci o odgovornosti

Lucić Vrdoljak, Ana ; Čalić, Maja ; Radić, Božica ; Berend, Suzana ; Jun, Daniel ; Kuča, Kamil ; Kovarik, Zrinka

engleski

Pretreatment with pyridinium oximes improves antidotal therapy against tabun poisoning

Oximes K033 [1, 4-bis(2-hydroxyiminomethylpyridinium) butane dibromide] and K048 [1-(4-hydroxyiminomethylpyridinium)-4-(4-carbamoylpyridinium) butane dibromide] were tested as pretreatment drugs in tabun poisoned mice followed by treatment with atropine plus K033, K048, K027 [1-(4-hydroxyiminomethylpyridinium)-3-(4-carbamoylpyridinium) propane dibromide], TMB-4 [1, 3-bis(4-hydroxyiminomethylpyridinium) propane dibromide] and HI-6 [(1-(2-hydroxyiminomethylpyridinium)-3-(4-carbamoylpyridinium)-2-oxapropane dichloride)]. Oxime doses of 25% or 5% of its LD50 were used for pretreatment 15 minutes before tabun-poisoning and for treatment one minute after tabun administration to mice. The best therapeutic effect was obtained when oxime K048 (25% of its LD50) was used in both pretreatment and treatment with atropine. This regiment insured survival of all tested animals after the application of 10 LD50 of tabun. In addition, since BChE is considered an endogenous bio-scavenger of anticholinesterase compounds and its interactions with oximes could be masked by AChE interactions, we evaluated kinetic parameters for interactions of tested oximes with native and tabun-inhibited human plasma butyrylcholinesterase (BChE ; EC 3.1.1.8) and compared them with results obtained previously for human erythrocyte acetylcholinesterase (AChE ; EC 3.1.1.7). Progressive inhibition of BChE by tabun was slightly faster than that of AChE. The reactivation of tabun-inhibited BChE by oximes was very slow, and BChE binding affinity for oximes was lower than AChE's. Therefore, BChE could scavenge tabun prior to AChE inhibition, but fast oxime-assisted reactivation of tabun-inhibited AChE or protection of AChE by oxime against inhibition with tabun would not be obstructed by interaction between BChE and oximes.

acetylcholinesterase; antidote; nerve agent; inhibition; reactivation; oxime; antidotal treatment

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Podaci o izdanju

228

2006.

41-50-x

objavljeno

0300-483X

Povezanost rada

Kemija

Indeksiranost