EC Number   |
Application |
Reference |
|---|
   1.17.3.2 | biotechnology |
construction of amperometric biosensors based in xanthine oxidase which has been immobilized by covalent binding to gold electrodes modified with dithiobis-N-succinimidyl propionate. Redox dyes thionine and methylene blue work well as electron acceptors for reduced enzyme |
671320 |
| 1.17.3.2 | diagnostics |
the enzyme activity detection in sepsis can be used for a negative prognosis in sepsis diagnosis, overview |
686134 |
| 1.17.3.2 | drug development |
the enzyme is a target for rational design of flavonoid-type inhibitors against xanthine oxidase useful for the treatment of hyperuricemia, gout, and inflammatory disease states |
745585 |
| 1.17.3.2 | medicine |
in Helicobacter pylori positive and negative pediatric patients, the activities of xanthine oxidase, myeloperoxidase, and superoxide dismutase in gastric mucosa are not affected by presence/absence of Helicobacter pylori |
675950 |
| 1.17.3.2 | medicine |
increased activity of xanthine oxidase in cells exposed to CoCl2 and subsequent increase in reactive oxygen species derived from enzyme activity, which results in accumulation of hypoxia-inducible factor 1alpha. Blockade of enzyme activity by allopurinol, N-acetyl-L-cysteine or siRNA significantly attenuates expression of hypoxia-inducible factor 1alpha and thus the induction of genes such as erythropoietin and vascular endothelial growth factor |
672905 |
| 1.17.3.2 | medicine |
oral adminstration of cassia oil significantly reduces serum and hepatic urate levels in hyperuricemic mice. At 600 mg/kg, cassia oil is as potent as allopurinol. This hypouricemic effect is explained by inhibiting activities of liver xanthine oxidase and xanthine oxidoreductase |
675113 |
| 1.17.3.2 | pharmacology |
inhibition of xanthine oxidase is a potential therapeutic approach to diabetic neuropathy and vasculopathy |
686553 |
| 1.17.3.2 | pharmacology |
the enzyme is a target in treatment of heart failure |
687898 |
| 1.17.3.2 | synthesis |
the enzyme can be used for production of superoxide, from oxidation of an aldehyde, which in a co-oxidation system reacts with the aldehyde and converts beta-carotene to beta-ionone, method optimization, overview |
685728 |
