Acetylcholinesterase (Electric eel)

Acetylcholinesterase (Electric eel) (AChE) is a cholinergic enzyme primarily found at neuromuscular junctions and cholinergic synapses. The main function of acetylcholinesterase (Electric eel) is to catalyze the decomposition or hydrolysis of acetylcholine and other acetylcholine esters into acetic acid and choline, thereby terminating signal transmission between neurons and synapses, preventing the diffusion and activation of acetylcholine (ACh) nearby receptors, and is utilized in biochemical research^[1].

Under conditions of 37℃, 0.1 mol/L pH=8.0 phosphate buffer, the enzyme activity of acetylcholinesterase is measured by the amount of enzyme required to decompose 1 μmol of acetylthiocholine iodide (ATCI) per minute, defined as one unit of acetylcholinesterase activity.

Under certain conditions, organophosphates and carbamates inhibit the normal function of cholinesterase. The degree of inhibition is directly proportional to the concentration of pesticides. Normally, the enzyme catalyzes the hydrolysis of the neurotransmitter metabolite (acetylcholine), which reacts with a color developer to produce a yellow substance. The absorbance changes over time are measured using a spectrophotometer, and the inhibition rate is calculated. The presence of organophosphates and carbamates in the product can be determined by the inhibition rate.

References:

[1]. Israel Silman, et al. Acetylcholinesterase: how is structure related to function? Chem Biol Interact. 2008 Sep 25;175(1-3):3-10.