X4376
Xanthine Oxidase from bovine milk
lyophilized powder, 0.4-1.0 units/mg protein
Sinónimos:
XOD, Xanthine:oxygen oxidoreductase
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Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-657-6
MDL number:
Número CE:
1.17.3.2.
Specific activity:
0.4-1.0 units/mg protein
Biological source:
bovine milk
Servicio técnico
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Permítanos ayudarlebiological source
bovine milk
Quality Level
form
lyophilized powder
specific activity
0.4-1.0 units/mg protein
mol wt
283 kDa
composition
Protein, 10.0-25.0%
storage temp.
2-8°C
General description
Formerly E.C. 1.1.3.22
Application
Xanthine Oxidase from bovine milk has been used as a source for superoxide generation. It has also been used as a model enzyme in the internally calibrated electrochemical continuous enzyme assay (ICECEA).
Biochem/physiol Actions
The isoflavanoid genistein was shown to inhibit xanthine oxidase at concentrations between 0.1-4.0 μM and then activate xanthine oxidase at concentrations higher than 5 μM.
Xanthine oxidase is a molybdenum-containing enzyme that is found in the cytosol, and may be strongly inhibited by flavonoids. It plays a vital role in the metabolism of some drugs, as well as purines and pyrimidines. It is also known to be a biological source of reactive oxygen species.
Xanthine Oxidase acts as a potential biomarker for oxidative stress. It is also implicated in tissue and vascular injuries such as liver damage, inflammatory diseases and chronic heart failure.
Physical form
Contains 0.5% sodium salicylate.
Analysis Note
Protein determined by biuret
Other Notes
One unit will convert 1.0 μmole of xanthine to uric acid per min at pH 7.5 at 25 °C. Approx. 50% of the activity is obtained with hypoxanthine as substrate.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Clase de almacenamiento
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Product Information Sheet
Massimiliano Magro et al.
Materials (Basel, Switzerland), 13(7) (2020-04-16)
Generally, enzyme immobilization on nanoparticles leads to nano-conjugates presenting partially preserved, or even absent, biological properties. Notwithstanding, recent research demonstrated that the coupling to nanomaterials can improve the activity of immobilized enzymes. Herein, xanthine oxidase (XO) was immobilized by self-assembly
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Castoria R, et al.
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