Related Experiment Video
Updated: Aug 6, 2026

Direct Detection of the Acetate-forming Activity of the Enzyme Acetate Kinase
Published on: December 19, 2011
Ultraviolet spectrophotometric method for determination of cholinesterase activity with acetylcholine as a substrate
Abstract:
An enzymatic method for the determination of serum cholinesterase (ChE) activity is described. The method is based on the liberation of acetate from acetylcholine as a substrate by ChE and the conversion of the acetate to acetylphosphate and ADP in the presence of ATP by acetate kinase. The produced ADP is coupled with pyruvate kinase and lactate dehydrogenase in the presence of phosphoenolpyruvate and NADH. The amount of NADH consumed is determined by absorbance at 340 nm. The reaction proceeds stoichiometrically, and the dilution curve is linear up to 3300 U/liter. The results obtained by this method show a good correlation with those obtained by the usual methods.
Related Concept Videos
Direct-Acting Cholinergic Agonists: Chemistry and Structure-Activity Relationship
The direct-acting...
Direct-Acting Cholinergic Agonists: Pharmacokinetics
Cholinesterases: Distribution and Function
Indirect-Acting Cholinergic Agonists: Chemistry and Structure-Activity Relationship
Reversible inhibitors display short to medium durations of action. Short-acting agents include simple alcohols with...
Indirect-Acting Cholinergic Agonists: Mechanism of Action
Reversible inhibitors like edrophonium bind to a specific part of the enzyme called the anionic catalytic site. They form noncovalent bonds, which means they are not strongly attached to the enzyme. This creates a temporary and less stable enzyme–inhibitor complex, leading to...
Indirect-Acting Cholinergic Agonists: Pharmacokinetics
Reversible agents containing quaternary amines, such as neostigmine and edrophonium, are not easily absorbed orally because they are...

