Phosphylation kinetic constants and oxime‐induced reactivation in acetylcholinesterase from fetal bovine serum, bovine caudate nucleus, and electric eel-Reference-Cited by-同舟云学术

Phosphylation kinetic constants and oxime‐induced reactivation in acetylcholinesterase from fetal bovine serum, bovine caudate nucleus, and electric eel

Published:1991-09 Issue:1 Volume:34 Page:141-156
ISSN:0098-4108
Container-title:Journal of Toxicology and Environmental Health
language:en
Short-container-title:Journal of Toxicology and Environmental Health

Author:

Hanke Dan W.,Overton Michael A.

Publisher

Informa UK Limited

Subject

Pollution,Toxicology

Link

http://www.tandfonline.com/doi/pdf/10.1080/15287399109531554

Reference39 articles.

1. Some properties of specific cholinesterase with particular reference to the mechanism of inhibition by diethyl p-nitrophenyl thiophosphate (E 605) and analogues

2. Inhibition of acetylcholinesterase from different species by organophosphorus compounds, carbamates and methylsulphonylfluoride

3. Stereospecific reactivation by some hagedorn-oximes of acetylcholinesterases from various species including man, inhibited by soman

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4. Recent advances in evaluation of oxime efficacy in nerve agent poisoning by in vitro analysis;Toxicology and Applied Pharmacology;2007-03

5. Kinetic analysis of interactions between human acetylcholinesterase, structurally different organophosphorus compounds and oximes;Biochemical Pharmacology;2004-12