𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Reactivation of acetylcholinesterase inhibited by methamidophos and analogous (di)methylphosphoramidates

✍ Scribed by Leo P. A. Jong; Gre Z. Wolring; Hendrik P. Benschop

Publisher
Springer-Verlag
Year
1982
Tongue
English
Weight
516 KB
Volume
49
Category
Article
ISSN
0340-5761

No coin nor oath required. For personal study only.

πŸ“œ SIMILAR VOLUMES

Oxime-induced reactivation of acetylchol
Oxime-induced reactivation of acetylcholinesterase inhibited by organophosphinates
✍ D. W. Hanke; M. S. Beckett; M. A. Overton; C. K. Burdick; C. N. Lieske πŸ“‚ Article πŸ“… 1990 πŸ› John Wiley and Sons 🌐 English βš– 499 KB

Defense. Aherdeen Proving Ground. MD 21010-5425. USA K e y word5 organophosphinate, orgdnophosphonatc. harin, oxiiiieq ,icetylcholinesterasc. rexti\dtioii. pretrc'itment The comparative potency of oximes for reactivation of inhibited eel acetylcholinesterase (AChE) in vitro is dependent on the orga

Spontaneous and oxime-induced reactivati
Spontaneous and oxime-induced reactivation of acetylcholinesterase inhibited by phosphoramidates
✍ J. P. Langenberg; L. P. A. Jong; M. F. Otto; H. P. Benschop πŸ“‚ Article πŸ“… 1988 πŸ› Springer-Verlag 🌐 English βš– 593 KB

Methamidophos (CH3O(NH2)P(O)SCH3) and phosphoramidates, with the general structure RO(NH2)P(O)OC6H4-p-NO2, in which R = C2H5, C1CH2CH2, FCH2CH2 and F3CCH2, as well as (NH2)2P(O)OC6H4-p-NO2 were synthesized to investigate the relationship between the rates of inhibition and of spontaneous reactivatio

Inhibition of acetylcholinesterase by di
Inhibition of acetylcholinesterase by diisocyanates and its spontaneous reactivation
✍ Mahmoud Dewair; Xaver Baur; Rolf Mauermayer πŸ“‚ Article πŸ“… 1983 πŸ› Springer-Verlag 🌐 English βš– 275 KB

The inhibition of human acetylcholinesterase (AchE) by 4,4'-diphenylmethane diisocyanate (MDI) is determined and compared with the previously described inhibition of this enzyme by two other industrially used diisocyanates: toluene diisocyanate (TDI) and hexamethylene diisocyanate (HDI). The inhibit