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C3389

Sigma-Aldrich

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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About This Item

Numéro CAS:
9000-81-1
Numéro de classification (Commission des enzymes):
3.1.1.7 (BRENDA, IUBMB)
Numéro CE :
232-559-3
Numéro MDL:
MFCD00081268
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.77

Type

Type VI-S

Niveau de qualité

200

Forme

lyophilized powder

Activité spécifique

200-1,000 units/mg protein

Poids mol.

280 kDa

Composition

Protein, ≥45% biuret

Solubilité

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

Application(s)

diagnostic assay manufacturing

Température de stockage

−20°C

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Description générale

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.

Actions biochimiques/physiologiques

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

Définition de l'unité

One unit will hydrolyze 1.0 μmole of acetylcholine to choline and acetate per min at pH 8.0 at 37 °C.

Forme physique

Lyophilized powder containing Tris buffer salts

Notes préparatoires

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

Remarque sur l'analyse

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

Inhibiteur

Réf. du produit
Description
Tarif

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "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
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
Giuseppe Uras et al.
Frontiers in neuroscience, 15, 691222-691222 (2021-07-20)
Alzheimer's disease is a neurodegenerative disease characterized by disrupted memory, learning functions, reduced life expectancy, and locomotor dysfunction, as a result of the accumulation and aggregation of amyloid peptides that cause neuronal damage in neuronal circuits. In the current study
Acetylcholinesterase, I. Large-scale purification, homogeneity, and amino Acid analysis.
W Leuzinger et al.
Proceedings of the National Academy of Sciences of the United States of America, 57(2), 446-451 (1967-02-01)
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