Acetylcholinesterase (AChE) is an enzyme that breaks down the neurotransmitter acetylcholine into acetic acid and choline, thereby terminating nerve conduction. This enzyme is found in a variety of organisms, including humans, insects, mammals and so on. It can exert effects on organisms in different ways, such as participating in neural transmission, regulating blood flow, and controlling heart rate.

The biological activity of AChE is mainly reflected in its decomposition of acetylcholine. When acetylcholine secreted by neurons reaches receptors on the cell membrane, it triggers a series of reactions, thereby activating nerve conduction. However, when this reaction is completed, acetylcholine is broken down by AChE into harmless acetic acid and choline, thereby preventing sustained neural signal transmission.

There are many different methods available for detecting the activity of AChE. The most commonly used methods are colorimetric and electrochemical methods. The colorimetric method requires the use of a reactant to detect the rate of AChE decomposition of acetylcholine. This reactant may be a chemical fluorescent dye, color dye, enzyme marker, etc. During the reaction, the acetic acid and choline produced by the decomposition of acetylcholine can cause color changes in the reactants, which can be used to measure enzyme activity through spectroscopy or spectrophotometry.

Electrochemical methods determine the activity of enzymes by measuring the potential changes generated during the decomposition of acetylcholine. This method typically requires the use of electrochemical electrodes or sensors, followed by the addition of acetylcholine to the observed system. As the decomposition process progresses, the electrons released by acetylcholine will affect the potential of the observation electrode, allowing for the calculation of enzyme activity values.

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