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Merck

C1057

Sigma-Aldrich

Butyrylcholinesterase from equine serum

lyophilized powder, ≥900 units/mg protein

Sinónimos:

Acylcholine acyl-hydrolase, Choline esterase, butyryl, Pseudocholinesterase

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About This Item

Número de CAS:
Comisión internacional de enzimas:
Número CE:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54

Formulario

lyophilized powder

Nivel de calidad

actividad específica

≥900 units/mg protein

mol peso

tetramer 440 kDa

composición

Protein, ≥10%

solubilidad

H2O: soluble 10 mg/mL

aplicaciones

diagnostic assay manufacturing

temp. de almacenamiento

−20°C

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Aplicación

Selective inhibition of BChE activity can be used in the detection of organophosphates. Its use in the treatment of organophosphate toxicity has been explored. It has been reported that the level of BChE in human blood correlates to the degree of protection against potentially toxic nerve agents. Cholinesterases have also been investigated for their role in Alzheimer′s disease.

Acciones bioquímicas o fisiológicas

Butyrylcholinesterase (BChE) is a serine hydrolase that is structurally similar to acetylcholinesterase (AChE), but differs in substrate specificities and inhibitor sensitivities.BChE can, unlike AChE, efficiently hydrolyze larger esters of choline such as butyrylcholine and benzoylcholine. The enzyme is a tetrameric glycoprotein with four equal subunits (110 kDa each). The enzyme is activated by Ca2+ and Mg2+. The activity is constant over the pH range of 6.0-8.0. It is inhibited by betaine, nicotine, organophosphates, and carbamate.

Definición de unidad

One unit will hydrolyze 1.0 μmole of butyrylcholine to choline and butyrate per min at pH 8.0 at 37 °C. The activity obtained using butyrylcholine as substrate is ~2.5 times that obtained using acetylcholine.

Forma física

Highly purified; contains buffer salts

Nota de análisis

Protein determined by biuret

Inhibidor

Referencia del producto
Descripción
Precios

Pictogramas

Health hazard

Palabra de señalización

Danger

Frases de peligro

Consejos de prudencia

Clasificaciones de peligro

Resp. Sens. 1

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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Tarek Mohamed et al.
Bioorganic & medicinal chemistry letters, 20(12), 3606-3609 (2010-05-18)
A group of 2,4-disubstituted pyrimidine derivatives (7a-e, 8a-e and 9a-d) that possess a variety of C-2 aliphatic five- and six-membered heterocycloalkyl ring in conjunction with a C-4 arylalkylamino substituent were designed, synthesized and evaluated as cholinesterase (ChE) inhibitors. The steric
Keriman Ozadali-Sari et al.
Bioorganic chemistry, 72, 208-214 (2017-05-10)
The present study describes the synthesis, pharmacological evaluation (BChE/AChE inhibition, Aβ antiaggregation, and neuroprotective effects), and molecular modeling studies of novel 2-[4-(4-substitutedpiperazin-1-yl)phenyl]benzimidazole derivatives. The alkyl-substituted derivatives exhibited selective inhibition on BChE with varying efficiency. Compounds 3b and 3d were found
Jianhua Liu et al.
The Journal of clinical endocrinology and metabolism, 93(5), 1980-1987 (2008-03-20)
Ghrelin, an acylated peptide hormone secreted from the gut, regulates appetite and metabolism. Elucidating its pattern of secretion in the fed and fasted states is important in the face of the obesity epidemic. Our objective was to examine changes in
R M Blong et al.
The Biochemical journal, 327 ( Pt 3), 747-757 (1998-05-15)
Butyrylcholinesterase (BChE) in human serum consists predominantly of tetramers. Recombinant BChE, however, expressed in Chinese hamster ovary (CHO) cells, consists of approx. 55% dimers, 10-30% tetramers and 15-40% monomers. To determine the origin of the monomer species we added the
Determination of butyrylcholinesterase inhibition using ion transfer across the interface between two immiscible liquids
Beattie PD, et al.
Analytical Chemistry, 66(1), 52-57 (1994)

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