C2629
Acetylcholinesterase from Electrophorus electricus (electric eel)
Type III, aqueous solution, ≥1,000 units/mg protein
Synonym(s):
AChE, Acetylcholine acetylhydrolase, Cholinesterase, Acetyl
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About This Item
CAS Number:
UNSPSC Code:
12352200
EC Number:
232-559-3
MDL number:
type
Type III
form
aqueous solution
specific activity
≥1,000 units/mg protein
impurities
~5 mg/mg protein (NH4)2SO4
color
clear to slightly hazy light yellow
shipped in
dry ice
storage temp.
−20°C
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General description
Molecular Weight: 280 kDa
Isoelectric Point: 5.5
Extinction Coefficient: E1% = 18.0 (280 nm)
Acetylcholinesterase from Electrophorus electricus is a tetramer composed of 4 equal subunits of 70 kDa each. Each subunit contains one active site. The enzyme is a glycoprotein containing hexosamines.
Isoelectric Point: 5.5
Extinction Coefficient: E1% = 18.0 (280 nm)
Acetylcholinesterase from Electrophorus electricus is a tetramer composed of 4 equal subunits of 70 kDa each. Each subunit contains one active site. The enzyme is a glycoprotein containing hexosamines.
Biochem/physiol Actions
Major degradative enzyme for acetylcholine in vivo. Converts acetylcholine + H2O to choline + acetic acid.
Analysis Note
The activity obtained using acetylcholine as substrate is 30-100 times that obtained with butyrylcholine, using acetylcholinesterase from electric eel.
Other Notes
One unit will hydrolyze 1.0 μmole of acetylcholine to choline and acetate per min at pH 8.0 at 37 °C.
Disclaimer
Excellent stability while frozen; avoid repeated freeze-thaw cycles.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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H Soreq et al.
Proceedings of the National Academy of Sciences of the United States of America, 87(24), 9688-9692 (1990-12-01)
To study the primary structure of human acetylcholinesterase (AcChoEase; EC 3.1.1.7) and its gene expression and amplification, cDNA libraries from human tissues expressing oocyte-translatable AcChoEase mRNA were constructed and screened with labeled oligodeoxynucleotide probes. Several cDNA clones were isolated that
R Karpel et al.
Experimental cell research, 210(2), 268-277 (1994-02-01)
To study the molecular mechanisms underlying the intensive expression of acetylcholinesterase (AChE) in different tumor types, we characterized levels and composition of its messenger RNA (mRNA) sequences in heterologous tumor cell lines, primary tumor biopsies, and normal fetal and adult
C F Bartels et al.
American journal of human genetics, 52(5), 928-936 (1993-05-01)
Acetylcholinesterase is present in innervated tissues, where its function is to terminate nerve impulse transmission. It is also found in the red blood cell membrane, where its function is unknown. We report the first genetic variant of human acetylcholinesterase and
Maria Gonzalez-Rey et al.
Aquatic toxicology (Amsterdam, Netherlands), 148, 221-230 (2014-02-15)
In recent years, research studies have increasingly focused on assessing the occurrence of active pharmaceutical ingredients (APIs) in ecosystems. However, much remains unknown concerning the potential effects on APIs on non-target organisms due to the complexity of the mode of
Colin J Jackson et al.
Toxicology, 317, 1-5 (2014-01-23)
Organophosphorus (OP) pesticides are a diverse class of acetylcholinesterase (AChE) inhibitors that are responsible for tremendous morbidity and mortality worldwide, killing approximately 300,000 people annually. Enzymatic hydrolysis of OPs is a potential therapy for acute poisoning. OpdA, an OP hydrolase
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