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C7512

Sigma-Aldrich

Butyrylcholinesterase from equine serum

lyophilized powder, ≥10 units/mg protein

Synonym(s):

Acylcholine acyl-hydrolase, Choline esterase, butyryl, Pseudocholinesterase

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

form

lyophilized powder

specific activity

≥10 units/mg protein

mol wt

tetramer 440 kDa

composition

Protein, ≥60%

solubility

cold water: 60 U/mL

storage temp.

−20°C

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General description

Butyrylcholinesterase (BChE) is a serine hydrolase that is structurally similar to acetylcholinesterase (AChE), but differs in substrate specificities and inhibitor sensitivities. The enzyme is a tetrameric glycoprotein with four equal subunits (110 kDa each). It is also termed as pseudocholinesterase. It is produced in the liver. It is found in blood, the synapse of neuromuscular junctions and glia cells and axons of white matter.

Application

Butyrylcholinesterase from equine serum has been used in a microcalorimetric study of the inhibition of butyrylcholinesterase by paraoxon. This enzyme has also been used in a study to investigate the synthesis and inhibition of cholinergic enzymes. Selective inhibition of BChE activity can be used in the detection of organophosphates. Its use in the treatment of organophosphate toxicity has shown clinical potential, as there is a correlation between the blood level of BChE in humans and the degree of protection against toxic nerve agents. There has also been an interest in the roles of cholinesterases with regard to Alzheimer′s disease. Investigations into selective inhibitors may provide a clearer picture of the physiological role of BChE in both healthy and diseased individuals. This product has been used for the screening of cholineesterase inhibitors in selected fruits and vegetables, for restoring cognitive function and improving memory. It has also been used to develop a butyrylcholinesterase and choline oxidase immobilized bio-sniffer for the detection of nicotine. Nicotine inhibits BChE activity. A decrease in the byproducts of BChE activity reflects the volume of nicotine.

Biochem/physiol Actions

Butyrylcholinesterase (BChE) can, unlike AChE, efficiently hydrolyze larger esters of choline such as butyrylcholine and benzoylcholine. The enzyme is activated by Ca2+ and Mg2+ and the activity is constant over the pH range 6.0-8.0. It is inhibited by betaine, nicotine, organophosphates, and carbamates.
Mutations in butyrylcholinesterase (BChE) gene results in the failure of respiratory system, prolonged paralysis and apnea.

Unit Definition

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.

Physical form

Lyophilized powder containing buffer salts

Preparation Note

This product is prepared from equine serum using ammonium sulfate fractionation and supplied as a lyophilized powder.

Analysis Note

Protein determined by biuret

inhibitor

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Toxicokinetics of Chemical Warfare Agents: Nerve Agents and Vesicants
Handbook of Toxicology of Chemical Warfare Agents, 755-790 (2009)
Kohji Mitsubayashi et al.
Analytica chimica acta, 573-574, 69-74 (2007-08-29)
A novel bioelectronic sniffer for nicotine in the gas phase was developed with enzyme inhibition principle to butyrylcholinesterase activity. The bioelectronic devices for nicotine in the gas and liquid phases were constructed using a Clark-type dissolved oxygen electrode and a
Screening for cholinesterase inhibitors in selected fruits and vegetables.
Szwajgier D and Borowiec K
Biotechnology, 15(2) (2012)
Determinants of intracellular pH in the erythrocyte.
J Warth et al.
British journal of haematology, 29(3), 369-372 (1975-03-01)
Population-scale genomics-Enabling precision public health
Advances in Genetics, 103, 119-161 (2019)

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