C0663
Acetylcholinesterase from human erythrocytes
buffered aqueous solution, ≥500 units/mg protein (BCA)
Sinónimos:
AChE, Acetylcholine acetylhydrolase
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Descripción general
Acetylcholinesterase (AChE) belongs to the carboxyl esterase family of enzymes. The erythrocyte AChE is membrane bound. AChE is mapped to human chromosome 7q22.1. It is enriched in aged erythrocytes.
Predominantly exists as a tetrameric glycoprotein composed of disulfide-linked homodimers with a monomer MW of ~80 kDa.
Aplicación
Acetylcholinesterase (AChE) from Sigma has been used in the structure-activity study of phosphoramido acid esters as inhibitors of AChE.
Acetylcholinesterase from human erythrocytes has been used in:
- cholinesterase inhibition assay for screening 4-aminoquinoline based compounds
- AChE activity assays to test the effect of positive allosteric modulators (PAMs)
- organophosphorus compounds based inhibition assay
Acciones bioquímicas o fisiológicas
Acetylcholinesterase (AChE) is regarded as a biomarker in neurotoxicity. It is a modulator of nitric oxide signal transduction pathway and marker of membrane integrity and aging. The levels of erythrocyte (RBC) AChE are affected on pesticide exposure and in hemolytic anemia. RBC AChE is a marker in Hirschsprung′s disease and inflammation.
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. 3.1.1.7], the serum associated enzyme, which is Pseudocholinesterase or Butyrylcholinesterase [(BuChE) - EC 3.1.1.8].
AChE is an ectoenzyme, anchored to the erythrocyte membrane via a GPI moiety.
AChE is an ectoenzyme, anchored to the erythrocyte membrane via a GPI moiety.
Major degradative enzyme for acetylcholine in vivo. Converts acetylcholine + H2O to choline + acetic acid.
Definición de unidad
One unit will hydrolyze 1.0 μmole of acetylthiocholine iodide per min at pH 7.4 at 37 °C.
Forma física
Solution in 20 mM HEPES, pH 8.0, containing 0.1% TRITON® X-100
Nota de preparación
The enzyme is the amphiphilic form extracted together with its GPI anchor with the aid of TRITON X-100 and purified by affinity chromatography.
Nota de análisis
The activity obtained using acetylcholine as substrate is 30-100 times that obtained with butyrylcholine, using acetylcholinesterase from electric eel.
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
Eyeshields, Gloves, type N95 (US)
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Los clientes también vieron
Synthesis, lipophilicity study and in vitro evaluation of some rodenticides as acetylcholinesterase reversible inhibitors
Ghadimi S, et al.
Journal of Enzyme Inhibition and Medicinal Chemistry, 23(2), 213-217 (2008)
Acetylcholinesterase from human erythrocytes as a surrogate biomarker of lead induced neurotoxicity
Gupta VK, et al.
Enzyme Research, 2015 (2015)
High-Throughput Screening for Positive Allosteric Modulators Identified Potential Therapeutics against Acetylcholinesterase Inhibition
Chapleau RR, et al.
Journal of Biomolecular Screening, 20(9), 1142-1149 (2015)
Saied Ghadimi et al.
Journal of enzyme inhibition and medicinal chemistry, 23(4), 556-561 (2008-07-31)
Phosphoramido acid esters (CH(3))(2)NP(O)X(p-OC(6)H(4)-CH(3)) (containing P-Cl (1), P-O (2), P-F (3), P-CN (5), and P-N (4,6) bonds, X for 2, 4 and 6 is OCH(3), (C(2)H(5))(2)N and morpholin) have been synthesized to investigate the structure-activity study of AChE enzyme inhibition
Identification of 4-aminoquinoline core for the design of new cholinesterase inhibitors
Chen Y, et al.
PeerJ, 4, e2140-e2140 (2016)
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