C5896
Choline Oxidase from Alcaligenes sp.
lyophilized powder, ≥10 units/mg solid
Synonym(s):
Choline: oxygen 1-oxidoreductase
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50 UNITS
$109.00
100 UNITS
$200.00
500 UNITS
$589.00
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form
lyophilized powder
Quality Level
specific activity
≥10 units/mg solid
mol wt
~95 kDa
technique(s)
cell based assay: suitable
suitability
suitable for assay of choline
suitable for molecular biology
storage temp.
−20°C
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This Item | C4405 | C8868 | C1235 |
|---|---|---|---|
| technique(s) cell based assay: suitable | technique(s) - | technique(s) - | technique(s) - |
| specific activity ≥10 units/mg solid | specific activity 8-20 units/mg solid | specific activity ≥50 units/mg protein | specific activity ≥10 units/mg protein |
| form lyophilized powder | form lyophilized powder | form lyophilized powder | form lyophilized powder |
| suitability suitable for assay of choline, suitable for molecular biology | suitability - | suitability - | suitability - |
| mol wt ~95 kDa | mol wt 71 kDa by SDS-PAGE, 83 kDa by gel filtration | mol wt 64 kDa | mol wt 55 kDa |
| storage temp. −20°C | storage temp. −20°C | storage temp. −20°C | storage temp. −20°C |
General description
Isoelectric point:4.1 ± 0.1
Michaelis constants:2.84 x 10¯3M (Choline), 5.33 x 10¯3M (Betaine aldehyde)
Structure:One mol of FAD is covalently bound to mol of the enzyme
Inhibitors:p-Chloromercuribenzoate, Cu++, Co++, Hg++, Ag+
Optimum pH:8.0 – 8.5
Optimum temp:40 – 45°C
pH Stability:pH 7.0 – 9.0 (30°C, 2hr)
Thermal stability:Below 37°C (pH 7.5, 10min)
Michaelis constants:2.84 x 10¯3M (Choline), 5.33 x 10¯3M (Betaine aldehyde)
Structure:One mol of FAD is covalently bound to mol of the enzyme
Inhibitors:p-Chloromercuribenzoate, Cu++, Co++, Hg++, Ag+
Optimum pH:8.0 – 8.5
Optimum temp:40 – 45°C
pH Stability:pH 7.0 – 9.0 (30°C, 2hr)
Thermal stability:Below 37°C (pH 7.5, 10min)
Application
Choline oxidase from Alcaligenes sp. has been used:
- in a study to investigate a choline biosensor constructed with a chitinous membrane and its application in measuring cholinesterase inhibitory activities
- has also been used in spectroscopic studies on the photoreaction of choline oxidase with covalently bound flavin.
- as a component of phosphate buffer saline (PBS) buffer for measurement of choline acetyltransferase (ChAT) activity in brain tissue homogenates[1]
- to measure the choline generated by autotaxin (ATX) by ATX activity assay[2][3] and phospholipase-D (PLD) by PLD activity assay[4]
Biochem/physiol Actions
Choline oxidase catalyzes the four-electron oxidation of choline to glycine-betaine, with betaine-aldehyde as the intermediate and molecular oxygen as th eprimary electron acceptor. The enzyme can also accept betaine-aldehyde as a substrate. This allows the study of the reaction mechanism for the conversion of choline to the aldehyde intermediate, & of betaine-aldehyde to glycine-betaine.[5] The enzyme is a flavoprotein with a molecular weight of approx. 72,000 Da (gel filtration) or 66,000 Da (SDS gel electrophoresis).[6]
Other Notes
One unit will form 1 μmole of H2O2 with oxidation of 1 μmole of choline to betaine aldehyde per min at pH 8.0 at 37 °C. Note: During the conversion of choline to betaine by choline oxidase, 2 μmoles of H2O2 are produced for every μmole of choline.
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Description
Pricing
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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M Ohta-Fukuyama et al.
Journal of biochemistry, 88(1), 197-203 (1980-07-01)
Choline oxidase from Alcaligenes sp. catalyzed the oxidation of choline and betaine aldehyde to betaine with concomitant consumption of oxygen and production of hydrogen peroxide. The values of Km for choline and betaine aldehyde were 0.87 and 6.2 mM, respectively.
S Ikuta et al.
Journal of biochemistry, 82(6), 1741-1749 (1977-12-01)
Choline oxidase was purified from the cells of Arthrobacter globiformis by fractionations with acetone and ammonium sulfate, and column chromatographies on DEAE-cellulose and on Sephadex G-200. The purified enzyme preparation appeared homogeneous on disc gel electrophoresis. The enzyme was a
S Pundir et al.
Analytical biochemistry, 427(1), 26-32 (2012-05-09)
A bienzymatic choline biosensor was constructed by coimmobilizing acetylcholinesterase (AChE) and choline oxidase (ChO) onto nanocomposite of carboxylated multiwalled carbon nanotubes (c-MWCNTs) and zirconium oxide nanoparticles (ZrO(2)NPs) electrodeposited on the surface of a glassy carbon electrode (GCE) and using it
Giovanni Gadda
Biochimica et biophysica acta, 1646(1-2), 112-118 (2003-03-15)
Choline oxidase catalyzes the four-electron oxidation of choline to glycine-betaine, with betaine-aldehyde as intermediate and molecular oxygen as primary electron acceptor. The enzyme is capable of accepting betaine-aldehyde as a substrate, allowing the investigation of the reaction mechanism for both
Shihua Hou et al.
Biosensors & bioelectronics, 33(1), 44-49 (2012-01-11)
A novel acetylcholinesterase (AChE)/choline oxidase (ChOx) bienzyme amperometric acetylcholine biosensor based on gold nanoparticles (AuNPs) and multi-walled carbon nanotubes (MWCNTs) has been successfully developed by self-assembly process in combination of sol-gel technique. A thiolated aqueous silica sol containing MWCNTs and
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