Ugrás a tartalomra
Merck

C0663

Sigma-Aldrich

Acetylcholinesterase from human erythrocytes

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

Szinonimák:

AChE, Acetylcholine acetylhydrolase

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

CAS-szám:
Enzyme Commission szám:
EC-szám:
MDL-szám:
UNSPSC kód:
12352204
NACRES:
NA.54

biológiai forrás

human erythrocytes

Minőségi szint

form

buffered aqueous solution

specifikus aktivitás

≥500 units/mg protein (BCA)

molekulatömeg

~80 kDa

UniProt elérési szám

tárolási hőmérséklet

2-8°C

Géninformáció

human ... ACHE(43)

Általános leírás

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.

Alkalmazás

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

Biokémiai/fiziológiai hatások

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.

Egység definíció

One unit will hydrolyze 1.0 μmole of acetylthiocholine iodide per min at pH 7.4 at 37 °C.

Fizikai forma

Solution in 20 mM HEPES, pH 8.0, containing 0.1% TRITON® X-100

Elkészítési megjegyzés

The enzyme is the amphiphilic form extracted together with its GPI anchor with the aid of TRITON X-100 and purified by affinity chromatography.

Analízis megjegyzés

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

Tárolási osztály kódja

11 - Combustible Solids

WGK

WGK 3

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable

Egyéni védőeszköz

Eyeshields, Gloves, type N95 (US)


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

Már rendelkezik ezzel a termékkel?

Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.

Dokumentumtár megtekintése

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)
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
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)
Variability of AChE, BChE, and ChAT genes in the late-onset form of Alzheimer's disease and relationships with response to treatment with Donepezil and Rivastigmine
Scacchi R, et al.
American Journal of Medical Genetics. Part B, Neuropsychiatric Genetics : the Official Publication of the International Society of Psychiatric Genetics, 150(4), 502-507 (2009)
Acetylcholinesterase from human erythrocytes as a surrogate biomarker of lead induced neurotoxicity
Gupta VK, et al.
Enzyme Research, 2015 (2015)

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