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X4500

Sigma-Aldrich

Xanthine Oxidase from bovine milk

Grade III, ammonium sulfate suspension, ≥0.8 units/mg protein

Synonym(s):

Schardinger enzyme, XnOx, hypoxanthine oxidase, 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

Quality Level

type

Grade III

form

ammonium sulfate suspension

specific activity

≥0.8 units/mg protein

technique(s)

inhibition assay: suitable

color

faint brown to dark brown

UniProt accession no.

foreign activity

uricase ≤0.1%

storage temp.

2-8°C

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General description

Research area: Cell Cycle

Xanthine Oxidase (XO) belongs to the class of complex metalloflavoproteins. It is produced by oxidation of sulfhydryl residues or by proteolysis of xanthine dehydrogenase (XDH). XO is characterized with two flavin molecules (FAD), two molybdenum atoms, and eight iron atoms bound per enzymatic unit.
Formerly E.C. 1.1.3.22

Application

Xanthine Oxidase from bovine milk has been used:
  • as a source for superoxide generation
  • for the degradation of hypoxanthine
  • for the detection of reactive oxygen species (ROS) in lipid model by electron spin resonance (ESR) spin trap method
  • as a constituent of assay mixture in xanthine oxidase inhibition assay

Biochem/physiol Actions

Xanthine Oxidase (XO)catalyzes the hydroxylation of hypoxanthine to xanthine and xanthine to uric acid. Xanthine oxidase activity is inhibited by folic acid. [7] and various other inhibitors including 3,4-Dihydroxy-5-nitrobenzaldehyde (DHNB), febuxostat and allopurinol. XO and xanthine dehydrogenase (XDH) plays a vital role in the last two steps in the formation of urate. Elevated levels of XO has been observed in the serum of chronic liver disease patients. Therefore, XO can be used as a biomarker for the detection of liver disease.
Xanthine oxidase activity is inhibited by folic acid.
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

Suspension in 2.3 M (NH4)2SO4, 10 mM sodium phosphate buffer, pH 7.8, containing 1 mM EDTA and 1 mM sodium salicylate

Preparation Note

Chromatographically purified

Storage and Stability

Tightly closed. Dry. Keep locked up or in an area accessible only to qualified or authorized
persons

Analysis Note

Protein determined by biuret

substrate

Product No.
Description
Pricing

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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C Y Ho et al.
The Journal of nutrition, 106(11), 1600-1609 (1976-11-01)
The effects of acidic and intestinal proteolytic environments on bovine milk xanthine oxidase (XO) activity were determined in order to evaluate the extent to which this enzyme was absorbed in biologically active form. The inhibition of XO by folic acid
Andrija Šmelcerović et al.
European journal of medicinal chemistry, 135, 491-516 (2017-05-10)
Xanthine oxidase (XO), a versatile metalloflavoprotein enzyme, catalyzes the oxidative hydroxylation of hypoxanthine and xanthine to uric acid in purine catabolism while simultaneously producing reactive oxygen species. Both lead to the gout-causing hyperuricemia and oxidative damage of the tissues where
Purification of immunomodulatory factors in human peripheral blood leukocytes
Montecucchi PC, et al.
Journal of Chromatography A, 512(8), 139-147 (1990)
Serum xanthine oxidase in human liver disease
Battelli M, et al.
The American Journal of Gastroenterology, 96(4), 1194-1199 (2001)
Detection of superoxide anion radical in a stratum corneum intercellular lipid model using an electrochemical sensor
Kaneko T, et al.
Journal of Oleo Science, 60(12), 647-654 (2011)

Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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