Naslov
Reactivation of phosphonylated acetylcholinesterase analyzed by chirality and mutagenesis

Autori
Kovarik, Zrinka ; Radić, Zoran ; Berman, Harvey A. ; Simeon-Rudolf, Vera ; Reiner, Elsa ; Taylor, Palmer

Vrsta, podvrsta i kategorija rada
Radovi u zbornicima skupova, cjeloviti rad (in extenso), znanstveni

Izvornik
Proceedings of Eight International Symposium on Protection against Chemical and Biological Warfare Agents / Puu, Gertrud - Umeå : FOI-Swedish Defence Research Agency, 2004

Skup
Eight International Symposium on Protection against Chemical and Biological Warfare Agents

Mjesto i datum
Göteborg, Švedska, 02.06.2004. - 06.06.2004

Vrsta sudjelovanja
Predavanje

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
acetylcholinesterase; inhibition; organophosphorus compound; oxime

Sažetak
Selective mutants of mouse acetylcholinesterase (AChE ; EC 3.1.1.7) phosphonylated with chiral SP- and RP-cycloheptyl, -3, 3-dimethylbutyl and -isopropyl, methylphosphonyl thiocholines were subjected to reactivation by the oximes HI-6 and 2-PAM and their reactivation kinetics compared with wild-type AChE. Obtained reactivation rates reach values sufficient for consideration of mixtures of a mutant enzyme and an oxime as a scavenging strategy in protection and treatment of organophosphate exposure. The enhanced scavenging capacity is manifested to the greatest extent in those bulky SP enantiomers that are most intractable to reactivation. Methylphosphonates, cyclosarin and soman, would fall into that category.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

POVEZANOST RADA