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C0663 Sigma

Acetylcholinesterase from human erythrocytes

buffered aqueous solution, ≥500 units/mg protein (BCA)

Synonym: AChE, Acetylcholine acetylhydrolase



Analysis Note

The activity obtained using acetylcholine as substrate is 30-100 times that obtained with butyrylcholine, using acetylcholinesterase from electric eel.

Preparation Note

The enzyme is the amphiphilic form extracted together with its GPI anchor with the aid of TRITON X-100 and purified by affinity chromatography.

Unit Definition

One unit will hydrolyze 1.0 μmole of acetylthiocholine iodide per min at pH 7.4 at 37 °C.

Physical form

Solution in 20 mM HEPES, pH 8.0, containing 0.1% TRITON® X-100


Acetylcholinesterase (AChE) from Sigma has been used in the structure-activity study of phosphoramido acid esters as inhibitors of AChE.

Biochem/physiol Actions

Acetylcholinesterase is the major in vivo degradative enzyme for acetylcholine. It converts acetylcholine and water to choline and acetic acid. Cholinesterases are inhibited by the natural carbamate alkaloid, eserine or physostigmine.

In blood there are two cholinesterases present: The erythrocyte associated enzyme, which is a true cholinesterase or acetylcholinesterase [(AChE) - E.C.], the serum associated enzyme, which is Pseudocholinesterase or Butyrylcholinesterase [(BuChE) - EC].
AChE is an ectoenzyme, anchored to the erythrocyte membrane via a GPI moiety.

General description

Predominantly exists as a tetrameric glycoprotein composed of disulfide-linked homodimers with a monomer MW of ~80 kDa.

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