Enzymatic assay
| Efficacy type: | Vmax slope (OD/min) Maximum ACh hydrolyzation |
| Stock solution: | 20 mM in DMSO |
| Compound quantity | < 1 mg |
In Brief:
Acetylcholinesterase (AChE) is a serine hydrolase mainly found at neuromuscular junctions and cholinergic brain synapses.
AChE hydrolyzes choline esters. Its principal biological role is termination of impulse transmission at cholinergic synapses, by rapid hydrolysis of the neurotransmitter acetylcholine to acetate and choline. Organophosphorus poisons form covalent bonds with a serine residue at the active site of AChE, and are thus potent irreversible inhibitors of AChE. AChE inhibitors prevent cholinesterase from breaking down acetylcholine, increasing both the level and duration of the neurotransmitter action. The assay is based on the Ellman method in which thiocholine, produced by AChE, reacts with 5,5’-dithiobis (2-nitrobenzoic) acid (DTNB) to form a colorimetric (412 nm) product, the5-thio-2-nitrobenzoate (TNB), proportional to the AChE activity present.
Definitions:
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