Description
Analysis Note The activity obtained using acetylcholine as substrate is 30-100 times that obtained with butyrylcholine, using acetylcholinesterase from electric eel.
Biochem/physiol Actions Major degradative enzyme for acetylcholine in vivo. Converts acetylcholine + H2O to choline + acetic acid.
General description Molecular Weight: 280 kDa
Isoelectric Point: 5.5
Extinction Coefficient: E1% = 18.0 （280 nm）

Acetylcholinesterase from Electrophorus electricus is a tetramer composed of 4 equal subunits of 70 kDa each. Each subunit contains one active site. The enzyme is a glycoprotein containing hexosamines.
Unit Definition One unit will hydrolyze 1.0 μmole of acetylcholine to choline and acetate per min at pH 8.0 at 37 °C.
Physical form Lyophilized powder containing Tris buffer salts

Properties
type Type VI-S
form lyophilized powder
composition Protein, ≥60% biuret 
storage temp. −20°C

Safety
Personal Protective Equipment Eyeshields, Gloves, type N95 （US）, type P1 （EN143） respirator filter
WGK Germany 3

References
reference Levinson, S., and Ellory, J., The molecular form of acetylcholinesterase as determined by irradiation inactivation. Biochem. J. 137, 123-125, （1974）
  Rosenberry, T.L., et al., Structure of the 11S acetylcholinesterase. Subunit composition. Biochemistry 13, 3068-3079, （1974）
  Anglister, I., and Silman, I., Molecular structure of elongated forms of electric eel acetylcholinesterase. J. Mol. Biol. 125, 293-311, （1978）
  Taylor, P., The cholinesterases. J. Biol. Chem. 266, 4025-4028, （1991）
  Froede, H.C., and Wilson I.B., Direct determination of acetyl-enzyme intermediate in the acetylcholinesterase-catalyzed hydrolysis of acetylcholine and acetylthiocholine. J. Biol. Chem. 259, 11010-11013, （1984）
  Szegletes, T., et al., Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis. Substrate inhibition arises as a secondary effect. Biochemistry 38, 122-133, （1999）

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