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X4376

Sigma-Aldrich

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:
Enzyme Commission number:
1.17.3.2.
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bovine milk

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

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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 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.
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.

Unit Definition

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.

Physical form

Contains 0.5% sodium salicylate.

Analysis Note

Protein determined by biuret

pictograms

Health hazard

signalword

Danger

hcodes

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)


Certificates of Analysis (COA)

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Rapid electrochemical enzyme assay with enzyme-free calibration
Zhang M, et al.
Analytical Chemistry, 85(12), 6026-6032 (2013)
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
Resistance of postharvest biocontrol yeasts to oxidative stress: a possible new mechanism of action
Castoria R, et al.
Phytopathology, 93(5), 564-572 (2003)
Rokshana Sharmin et al.
ACS sensors, 6(12), 4349-4359 (2021-11-20)
Free-radical generation is suspected to play a key role in cardiovascular diseases. Another crucial factor is shear stress. Human umbilical vein endothelial cells (HUVECS), which form the lining of blood vessels, require a physiological shear stress to activate many vasoactive
Kathrin S Zeller et al.
PloS one, 8(5), e64897-e64897 (2013-06-06)
Cells are exposed to several types of integrin stimuli, which generate responses generally referred to as "integrin signals", but the specific responses to different integrin stimuli are poorly defined. In this study, signals induced by integrin ligation during cell attachment

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