Srovnávání schopnosti nově vyvinutých oximů (K005, K027, K033, K048) a současně užívaných oximů (pralidoxim, obidoxim, HI-6) při reaktivaci sarinem-i nhibované acetylcholinesterázy krysího mozku metodou in vitro

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60162694%3AG44__%2F05%3A00001309" target="_blank" >RIV/60162694:G44__/05:00001309 - isvavai.cz</a>

Výsledek na webu

—

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

A comparison of the potency of newly developed oximes (K005, K027, K033, K048) and currently used oximes (pralidoxime, obidoxime, HI-6) to reactivate sarin-inhibited rat brain acetylcholinesterase by in vitro methods

Popis výsledku v původním jazyce

A potency of newly developed and currently used oximes to reactivate sarin-inhibited acetylcholinesterase was evaluated using in vitro methods. A rat brain homogenate was taken as a source of acetylcholinesterase. Significant differences in reactivationpotency among all tested oximes were observed. Although the ability of newly developed oximes to reactivate sarin-inhibited acetylcholinesterase does not reach the reactivating potency of the oxime HI-6, the oxime K033 seems to be more efficacious reactivator of sarin-inhibited acetylcholinesterase than other currently available oximes (pralidoxime, obidoxime) at concentrations (10-5 - 10-4 M) corresponding to recommended doses in vivo. The results of our study also confirm that the reactivation potencyof the tested reactivators depends on many factors - such as (1) the number of pyridinium rings, (2) the number of oxime groups and their position, and (3) the length and the shape of linkage bridge between both pyridinium rings.

Název v anglickém jazyce

A comparison of the potency of newly developed oximes (K005, K027, K033, K048) and currently used oximes (pralidoxime, obidoxime, HI-6) to reactivate sarin-inhibited rat brain acetylcholinesterase by in vitro methods

Popis výsledku anglicky

A potency of newly developed and currently used oximes to reactivate sarin-inhibited acetylcholinesterase was evaluated using in vitro methods. A rat brain homogenate was taken as a source of acetylcholinesterase. Significant differences in reactivationpotency among all tested oximes were observed. Although the ability of newly developed oximes to reactivate sarin-inhibited acetylcholinesterase does not reach the reactivating potency of the oxime HI-6, the oxime K033 seems to be more efficacious reactivator of sarin-inhibited acetylcholinesterase than other currently available oximes (pralidoxime, obidoxime) at concentrations (10-5 - 10-4 M) corresponding to recommended doses in vivo. The results of our study also confirm that the reactivation potencyof the tested reactivators depends on many factors - such as (1) the number of pyridinium rings, (2) the number of oxime groups and their position, and (3) the length and the shape of linkage bridge between both pyridinium rings.

Druh

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

CEP obor

FP - Ostatní lékařské obory

OECD FORD obor

—

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2005

Kód důvěrnosti údajů

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

Název periodika

Journal of Toxicology and Environmental Health

ISSN

0098-4108

e-ISSN

—

Svazek periodika

68

Číslo periodika v rámci svazku

8

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

10

Strana od-do

677-686

Kód UT WoS článku

—

EID výsledku v databázi Scopus

—