A comparison of the reactivating and therapeutic efficacy of two novel oximes K378 and K458 with currently available oximes in rats and mice poisoned with sarin

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60162694%3AG44__%2F14%3A43875133" target="_blank" >RIV/60162694:G44__/14:43875133 - isvavai.cz</a>

Výsledek na webu

<a href="http://www.sciencedirect.com/science/article/pii/S1214021X14000337#" target="_blank" >http://www.sciencedirect.com/science/article/pii/S1214021X14000337#</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.jab.2014.01.007" target="_blank" >10.1016/j.jab.2014.01.007</a>

Jazyk výsledku

angličtina

Název v původním jazyce

A comparison of the reactivating and therapeutic efficacy of two novel oximes K378 and K458 with currently available oximes in rats and mice poisoned with sarin

Popis výsledku v původním jazyce

The ability of two novel oximes K378 and K348 and currently available oximes (HI-6, obidoxime) to reactivate sarin-inhibited acetylcholinesterase and to reduce acute toxicity of sarin was evaluated. Both new potential oxime reactivators were chosen for this study based on the data obtained during the extensive work on oximes development, from structure-activity relationship studies and in vitro evaluation of their ability to reactivate acetylcholinesterase inhibited by organophosphorus compounds. In vivo determined percentage of reactivation of sarin-inhibited rat blood and brain acetylcholinesterase showed that the potency of both novel oximes K378 and K458 to reactivate sarin-inhibited acetylcholinesterase roughly corresponds to low reactivating efficacy of obidoxime. On the other hand, the oxime HI-6 was found to be efficient reactivator of sarin-inhibited acetylcholinesterase in the peripheral compartment. While the oxime HI-6 was able to reduce the acute toxicity of sarin more tha

Název v anglickém jazyce

A comparison of the reactivating and therapeutic efficacy of two novel oximes K378 and K458 with currently available oximes in rats and mice poisoned with sarin

Popis výsledku anglicky

The ability of two novel oximes K378 and K348 and currently available oximes (HI-6, obidoxime) to reactivate sarin-inhibited acetylcholinesterase and to reduce acute toxicity of sarin was evaluated. Both new potential oxime reactivators were chosen for this study based on the data obtained during the extensive work on oximes development, from structure-activity relationship studies and in vitro evaluation of their ability to reactivate acetylcholinesterase inhibited by organophosphorus compounds. In vivo determined percentage of reactivation of sarin-inhibited rat blood and brain acetylcholinesterase showed that the potency of both novel oximes K378 and K458 to reactivate sarin-inhibited acetylcholinesterase roughly corresponds to low reactivating efficacy of obidoxime. On the other hand, the oxime HI-6 was found to be efficient reactivator of sarin-inhibited acetylcholinesterase in the peripheral compartment. While the oxime HI-6 was able to reduce the acute toxicity of sarin more tha

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

FP - Ostatní lékařské obory

OECD FORD obor

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Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2014

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Applied Biomedicine - print

ISSN

1214-021X

e-ISSN

—

Svazek periodika

12

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

6

Strana od-do

155-160

Kód UT WoS článku

000340867600004

EID výsledku v databázi Scopus

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