Key Documents

View All Documentation

X1875

Xanthine Oxidase from bovine milk

Name: Xanthine Oxidase from bovine milk
Brand: SIGMA

Grade I, ammonium sulfate suspension, ≥0.4 units/mg protein

Synonym(s):

XOD, Xanthine:oxygen oxidoreductase

Select a Size

Change View

About This Item

CAS Number:

9002-17-9

UNSPSC Code:

12352204

NACRES:

NA.54

EC Number:

232-657-6

MDL number:

MFCD00082145

EC Number:

1.17.3.2.

Specific activity:

≥0.4 units/mg protein

Technical Service

Need help? Our team of experienced scientists is here for you.

Let Us Assist

Properties

type

Grade I

Quality Level

200

form

ammonium sulfate suspension

specific activity

≥0.4 units/mg protein

foreign activity

uricase ≤0.5%

shipped in

wet ice

storage temp.

2-8°C

Description

General description

Xanthine Oxidase (XOD) is a metal flavoprotein. It has flavin adenine dinucleotide (FAD), molybdenum and iron in the ratio 2:2:8. This homodimer has a molecule weight of 290kDa. It is a member of the molybdenum-protein family. This enzyme consists of two separated substrate-binding sites.

Formerly E.C. 1.1.3.22

Application

Xanthine Oxidase from bovine milk has been used:

in the preparation of xanthine oxidase (XO) solution for 5-(diethoxyphosphoryl)-5-methyl-1-pyrroline-N-oxide (DEPMPO)-spin trapping assay
in in vitro XO assay for screening Vietnamese medicinal plants for XO inhibitory activity
as a standard to determine XO activity
as a standard to test the synergistic effect of docosahexaenoic acid (DHA)

Biochem/physiol Actions

Hydroxylation of hypoxanthine to xanthine and xanthine to uric acid is catalyzed by xanthinebb oxidase (XO) enzyme.

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 was shown to be involved in the reduction of cytochrome c by the generation of superoxide anions following the oxidation of xanthine. These free radicals are responsible for reducing cytochrome c.

Physical form

Suspension in 2.3 M (NH₄)₂SO₄ containing 1 mM 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.