Effect of different buffers on kinetic properties of human acetylcholinesterase and the interaction with organophosphates and oximes

Author:

Wille T.,Thiermann H.,Worek F.

Publisher

Springer Science and Business Media LLC

Subject

Health, Toxicology and Mutagenesis,Toxicology,General Medicine

Reference43 articles.

1. Al-Jafari AA, Kamal MA (1996) Optimization and kinetic studies of human erythrocyte membrane- bound acetylcholinesterase. Biochem Mol Biol Int 38:577–586

2. Aurbek N, Thiermann H, Szinicz L, Eyer P, Worek F (2006) Analysis of inhibition, reactivation and aging kinetics of highly toxic organophosphorus compounds with human and pig acetylcholinesterase. Toxicology 224:91–99

3. Brestkin AP, Vyaz’menskaya MM, Maizel EB (1978) Influence of Triton X-100 on the properties of acetylcholinesterase from human erythrocytes. Biokhimiia 43:94–99

4. Chow CM, Islam MF (1970) Colorimetric determination of red blood cell acetylcholinesterase activity. Clin Biochem 3:295–306

5. Davies DR, Green AL (1956) The kinetics of reactivation, by oximes, of cholinesterase inhibited by organophosphorus compounds. Biochem J 63:529–535

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