Evaluation of 2,6-dichlorophenolindophenol acetate as a substrate for acetylcholinesterase activity assay
Jazyk angličtina Země Anglie, Velká Británie Médium print-electronic
Typ dokumentu časopisecké články
- Klíčová slova
- Acetylcholinesterase, Ellman method, assay, butyrylcholinesterase, chromogen, spectrophotometry, substrate,
- MeSH
- 2,6-dichlorindofenol chemická syntéza chemie farmakologie MeSH
- acetáty chemická syntéza chemie farmakologie MeSH
- acetylcholinesterasa metabolismus MeSH
- cholinesterasové inhibitory chemická syntéza chemie farmakologie MeSH
- lidé MeSH
- molekulární struktura MeSH
- vztah mezi dávkou a účinkem léčiva MeSH
- vztahy mezi strukturou a aktivitou MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- 2,6-dichlorindofenol MeSH
- acetáty MeSH
- acetylcholinesterasa MeSH
- cholinesterasové inhibitory MeSH
Ellman's method is a standard protocol for the determination of cholinesterases activity. Though the method is ready for laboratory purposes, it has some drawbacks as well. In the current article, 2,6-dichloroindophenol acetate is performed as a chromogenic substrate suitable for acetylcholinesterase (AChE) activity examination. Michaelis constant and maximal velocity for 2,6-dichloroindophenol acetate were determined (38.0 µM and 244 pkat) and compared to the values for acetythiocholine (K(m) 0.18 mM; V(max) 5.1 nkat). Docking for 2,6-dichloroindophenol acetate and human AChE was done as well. In conclusion, 2,6-dichloroindophenol acetate seems to be suitable chromogenic substrate for AChE and spectrophotometry and based on this it can be easily performed whenever AChE activity should be tested.
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