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C3389

Sigma-Aldrich

Acetylcholinesterase from Electrophorus electricus (electric eel)

Type VI-S, lyophilized powder, 200-1,000 units/mg protein

Synonym(s):

AChE, Acetylcholine acetylhydrolase, Cholinesterase, Acetyl

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.77

type

Type VI-S

Quality Level

form

lyophilized powder

specific activity

200-1,000 units/mg protein

mol wt

280 kDa

composition

Protein, ≥45% biuret

solubility

20 mM Tris HCl buffer, pH 7.5: soluble 1.0 mg/mL, clear(lit.)

application(s)

diagnostic assay manufacturing

storage temp.

−20°C

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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.

Application

The enzyme from sigma has been used as a reference to to evaluate the effect of aspartame metabolites on hippocampal acetylcholinesterase activity. The enzyme has also been used in immobilization studies for the rapid detection of acetylthiocholine chloride.

Biochem/physiol Actions

Major degradative enzyme for acetylcholine in vivo. Converts acetylcholine + H2O to choline + acetic acid.

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

Preparation Note

This enzyme dissolves in 20 mM Tris-HCl buffer, pH 7.5 at 1 mg/mL concentration, yielding a clear solution.

Analysis Note

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

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Gabriela Villalta et al.
Plants (Basel, Switzerland), 10(6) (2021-07-03)
The essential oil (EO) of Salvia leucantha Cav. was isolated by steam distillation of the aerial parts collected in the South of Ecuador. Its physical properties were evaluated and the chemical composition of the oil was determined by GC-MS and
Makar Makarian et al.
Journal of molecular structure, 1247 (2022-03-01)
In an effort to develop new therapeutic agents to treat Alzheimer's disease, a series of donepezil-based analogs were designed, synthesized using an environmentally friendly route, and biologically evaluated for their inhibitory activity against electric eel acetylcholinesterase (AChE) enzyme. In vitro
Jingming Gong et al.
Biosensors & bioelectronics, 24(7), 2285-2288 (2008-12-30)
We developed a simple strategy for designing a highly sensitive electrochemical biosensor for organophosphate pesticides (OPs) based on acetylcholinesterase (AChE) immobilized onto Au nanoparticles-polypyrrole nanowires composite film modifid glassy carbon electrode (labeled as AChE-Au-PPy/GCE). Where, the generated Au nanoparticles (AuNPs)
Dan Du et al.
Biosensors & bioelectronics, 25(11), 2503-2508 (2010-05-18)
A simple method to immobilize acetylcholinesterase (AChE) on polypyrrole (PPy) and polyaniline (PANI) copolymer doped with multi-walled carbon nanotubes (MWCNTs) was proposed. The synthesized PAn-PPy-MWCNTs copolymer presented a porous and homogeneous morphology which provided an ideal size to entrap enzyme
Dan Du et al.
Analytical and bioanalytical chemistry, 387(3), 1059-1065 (2006-12-23)
A simple method has been devised for immobilization of acetylcholinesterase (AChE)--covalent bonding to a multiwall carbon nanotube (MWNT)--cross-linked chitosan composite (CMC)-and a sensitive amperometric sensor for rapid detection of acetylthiocholine (ATCl) has been based on this. Fourier-transform infrared spectroscopy proved

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