A spectrophotometric assay for determining the rate constants of acetylcholinesterase inhibitions
β Scribed by James K. Stoops; Myron L. Bender
- Publisher
- Elsevier Science
- Year
- 1975
- Tongue
- English
- Weight
- 625 KB
- Volume
- 63
- Category
- Article
- ISSN
- 0003-2697
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β¦ Synopsis
A spectrophotometric assay procedure has been developed for determining the rate constants for the inhibition of acetylcholinesterase by carbamates and phosphates. The method permits the investigation of inhibitors over a large range in the value of the phosphorylation or carbamylation rate constants without involving the kinetic parameters of the assay substrate in the calculations.
π SIMILAR VOLUMES
We have made a generalized treatment of first-order kinetic processes in dc polarography, obtaining approximate analytic expressions, applicable to any conditions. This treatment is applied to the electrochemical reduction of 0-nitrophenol, which undergoes a CECE mechanism in which both chemical sta
We have designed this study to determine various kinetic parameters of camel retinal membranebound acetylcholinesterase (AChE; EC 3.1.1.7) inhibition by carbamate insecticide lannate [methyl N-{{(methylamino)carbonyl}oxy} ethanimidothioate]. All these kinetic constants were derived by simple graphic