Izvorni znanstveni članak
Reactivation of phosphorylated cholinesterases in vitro and protecting effects in vivo of some pyridinium and quinolinium oximes
Vera Simeon
; Institute for Medical Research and Occupational Health, Yugoslav Academy of Sciences and Arts, Zagreb
Mira Škrinjarić-Špoljar
; Institute for Medical Research and Occupational Health, Yugoslav Academy of Sciences and Arts, Zagreb
Katja Wilhelm
; Institute for Medical Research and Occupational Health, Yugoslav Academy of Sciences and Arts, Zagreb
Sažetak
Six pyridinium and quinolinium oximes (I-VI) were tested as reactivators of serum and erythrocyte cholinesterases inhibited with 0-ethyl-S-(2-dimethylaminothioethyl)-methylphosphonate (medemo) and 0-ethyl p-nitrophenyl-ethylphosphonate (armin). They were also tested as protective agents in rats poisoned with l-methyl-2,2-dimethylpropylmethylphos-phonofluoridate (soman) and medemo. The results obtained were compared with the effect of TMB-4. Oxime IV [1.3 acetone-bis (4-pyridinium aldoxime)dichloride] proved to be a good reactivator of erythrocyte cholinesterase inhibited by medemo. Used as a protective agent together with atropine in rat poisoning it increased LD50 of medemo 48 times. Oximes I (1-benzyl-4-pyridinium aldoxime chloride) and III (l-phenacyloxime-2-pyridinium aldoxime chloride) were good reactivators of serum cholinesterase inhibited by armin and medemo. Oximes I and III used together with atropine raised LD50 in rats poisoned with medemo 20 times. Oximes III and II (l-phenacyloxime-2-pyridinium aldoxime chloride) used together with atropine increased LD50 in rats poisoned with soman 2.0 (oxime II) and 1.8 times (oxime III) respectively. Oximes V and VI (1-phenacyloxime-quinolinium chloride and 1-phenacyloxime-isoquinolinium chloride) were very toxic and did not reactivate inhibited cholinesterases at all. The effects of oximes tested were equal to or weaker than those of TMB-4 both in vitro and in viva studies.
Ključne riječi
Hrčak ID:
168186
URI
Datum izdavanja:
20.6.1973.
Posjeta: 1.231 *