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X4376

Xanthine Oxidase from bovine milk

lyophilized powder, 0.4-1.0 units/mg protein

Synonym(s):

XOD, Xanthine:oxygen oxidoreductase

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About This Item

CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-657-6
MDL number:
EC Number:
1.17.3.2.
Specific activity:
0.4-1.0 units/mg protein
Biological source:
bovine milk
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biological 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.[1] 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.

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1 of 1

This Item
X4875X450010110434001
specific activity

0.4-1.0 units/mg protein

specific activity

≥0.1 units/mg protein

specific activity

≥0.8 units/mg protein

specific activity

~1 units/mg protein (At 25 °C with xanthine as the substrate.)

biological source

bovine milk

biological source

bovine milk

biological source

bovine milk

biological source

bovine milk

form

lyophilized powder

form

ammonium sulfate suspension

form

ammonium sulfate suspension

form

suspension

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

mol wt

283 kDa

mol wt

-

mol wt

-

mol wt

-

Quality Level

300

Quality Level

200

Quality Level

200

Quality Level

-


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pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

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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Related Content


Rapid electrochemical enzyme assay with enzyme-free calibration
Zhang M, et al.
Analytical Chemistry, 85(12), 6026-6032 (2013)
Resistance of postharvest biocontrol yeasts to oxidative stress: a possible new mechanism of action
Castoria R, et al.
Phytopathology, 93(5), 564-572 (2003)
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



Global Trade Item Number

SKUGTIN
X4376-25UN04061837549694
X4376-50UN04061837549700
X4376-5UN04061837549717

Questions

  1. Good morning, I have a question how to use Xanthine Oxidase in the form lyophilized powder? In what form can it be used? Can it be converted into a liquid form? If so, what should be the solvent? Should I use water or buffer? If a buffer witch one?

    1 answer
    1. This enzyme is soluble in 50 mM potassium phosphate buffer at 1 mg/mL, yielding a clear solution. Please see the link below to review the product datasheet:
      https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/134/883/x4376pis.pdf

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