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Merck

X4500

Sigma-Aldrich

Xanthine Oxidase from bovine milk

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

Sinónimos:

Schardinger enzyme, XnOx, hypoxanthine oxidase, XOD, Xanthine:oxygen oxidoreductase

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About This Item

Número de CAS:
Comisión internacional de enzimas:
1.17.3.2.
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bovine milk

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.
enthält auch proteolytische Aktivität

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

Referencia del producto
Descripción
Precios

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)


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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)
Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion
Enroth C, et al.
Proceedings of the National Academy of Sciences of the USA, 97(20), 10723-10728 (2000)
Purification of immunomodulatory factors in human peripheral blood leukocytes
Montecucchi PC, et al.
Journal of Chromatography A, 512(8), 139-147 (1990)
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
Serum xanthine oxidase in human liver disease
Battelli M, et al.
The American Journal of Gastroenterology, 96(4), 1194-1199 (2001)

Artículos

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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