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Merck

C3389

Acetylcholinesterase from Electrophorus electricus (electric eel)

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

Synonyme(s) :

AChE, Acetylcholine acetylhydrolase, Cholinesterase, Acetyl

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A propos de cet article

Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.77
EC Number:
232-559-3
MDL number:
Numéro CE :
Specific activity:
200-1,000 units/mg protein
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Nom du produit

Acetylcholinesterase from Electrophorus electricus (electric eel), Type VI-S, lyophilized powder, 200-1,000 units/mg protein

type

Type VI-S

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

Quality Level

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Analysis Note

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

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.

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.

Other Notes

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.

Classe de stockage

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

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
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
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)
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
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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