C0663
Acetylcholinesterase from human erythrocytes
buffered aqueous solution, ≥500 units/mg protein (BCA)
Synonym(s):
AChE, Acetylcholine acetylhydrolase
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-559-3
MDL number:
Product Name
Acetylcholinesterase from human erythrocytes, buffered aqueous solution, ≥500 units/mg protein (BCA)
biological source
human erythrocytes
form
buffered aqueous solution
specific activity
≥500 units/mg protein (BCA)
mol wt
~80 kDa
UniProt accession no.
storage temp.
2-8°C
Quality Level
Gene Information
human ... ACHE(43)
General description
Predominantly exists as a tetrameric glycoprotein composed of disulfide-linked homodimers with a monomer MW of ~80 kDa.
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.
Other Notes
One unit will hydrolyze 1.0 μmole of acetylthiocholine iodide per min at pH 7.4 at 37 °C.
Physical form
Solution in 20 mM HEPES, pH 8.0, containing 0.1% TRITON® X-100
Preparation Note
The enzyme is the amphiphilic form extracted together with its GPI anchor with the aid of TRITON X-100 and purified by affinity chromatography.
Biochem/physiol Actions
Major degradative enzyme for acetylcholine in vivo. Converts acetylcholine + H2O to choline + acetic acid.
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.
Analysis Note
The activity obtained using acetylcholine as substrate is 30-100 times that obtained with butyrylcholine, using acetylcholinesterase from electric eel.
Application
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
Storage Class
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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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)
Acetylcholinesterase from human erythrocytes as a surrogate biomarker of lead induced neurotoxicity
Gupta VK, et al.
Enzyme Research, 2015 (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
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)
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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