Kinetic constants for the inhibition of camel retinal acetylcholinesterase by the carbamate insecticide lannate
✍ Scribed by Mohammad A. Kamal; Abdulaziz A. Al-Jafari
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 141 KB
- Volume
- 13
- Category
- Article
- ISSN
- 1095-6670
No coin nor oath required. For personal study only.
✦ Synopsis
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 graphical methods. The value of kinetic parameters was estimated as follows: 0.061 ( lM) 1 , 1.14 ( lM) 1 , 0.216 lM, 0.016 min 1 , 0.0741 ( lM min) 1 , 0.746 lM, and 4.42 lM for velocity constant (K v ), new inhibition constant (K nic ), dissociation constant (K d ), carbamylation rate constant (k 2c ), overall carbamylation rate constant ( ),
k 2 50% inhibition constant (K I50 ), and 99% inhibition constant (K I99 ), respectively. These unique methods may be used to estimate such kinetic parameters for time-dependent inhibition of enzymes by variety of chemicals, insecticides, herbicides, and drugs.