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MilliporeSigma

C0663

Acetylcholinesterase from human erythrocytes

buffered aqueous solution, ≥500 units/mg protein (BCA)

Synonym(s):

AChE, Acetylcholine acetylhydrolase

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50 UNITS

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About This Item

CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-559-3
MDL number:
EC Number:

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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)

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This Item
C1682SAB4200839MAB303
biological source

human erythrocytes

biological source

-

biological source

rabbit

biological source

mouse

specific activity

≥500 units/mg protein (BCA)

specific activity

≥1,000 units/mg protein (Lowry)

specific activity

-

specific activity

-

Gene Information

human ... ACHE(43)

Gene Information

human ... ACHE(43)

Gene Information

human ... ACHE(43)

Gene Information

human ... ACHE(43)

form

buffered aqueous solution

form

lyophilized powder

form

buffered aqueous solution

form

-

mol wt

~80 kDa

mol wt

64.6 kDa

mol wt

-

mol wt

-

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

-

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.[1] AChE is mapped to human chromosome 7q22.1.[2] It is enriched in aged erythrocytes.[3]

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.[1] It is a modulator of nitric oxide signal transduction pathway and marker of membrane integrity and aging.[3] 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.[3]
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.

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.[4]
Acetylcholinesterase from human erythrocytes has been used in:
  • cholinesterase inhibition assay for screening 4-aminoquinoline based compounds[5]
  • AChE activity assays to test the effect of positive allosteric modulators (PAMs)[6]
  • organophosphorus compounds based inhibition assay[7]

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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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
Human erythrocyte acetylcholinesterase in health and disease
Saldanha C
Molecules (Basel), 22(9), 1499-1499 (2017)

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