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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.
Product Name
Xanthine Oxidase from bovine milk, Grade III, ammonium sulfate suspension, ≥0.8 units/mg protein
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
Quality Level
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Analysis Note
Protein determined by biuret
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.
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.
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
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.
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
Tightly closed. Dry. Keep locked up or in an area accessible only to qualified or authorized
persons
persons
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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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)
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