Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.17.3.2 (xanthine oxidase)
 8,383 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Azelaic acid is an aliphatic dicarboxylic acid (HOOC-(CH2)7-COOH) which has recently been shown to have some practical therapeutic applications in skin diseases of different etiologies. It possesses diverse biological activities and its mechanisms of action are still under investigation. Azelaic acid, as disodium salt (C(9)2Na), at concentrations from 0.05 mM to 1.0 mM is capable of inhibiting significantly the hydroxylation of 1-tyrosine to 1-DOPA due to hydroxylradicals (HO.) produced by Fenton reaction. Similarly C(9)2Na significantly inhibits the heterogeneous photocatalytic oxidation of toluene to cresols, and the peroxidation of arachidonic acid (C20:4,n6), due to HO. formed by dissolved oxygen in the presence of UV-irradiated semiconductor TiO2 (photo-Fenton type reaction). C(9)2Na decomposition and its by-products formation are quantifiable only at high HO. concentrations. On the contrary, C(9)2Na is not a scavenger of O2-. generated by xanthine-xanthine oxidase system. Under the same experimental conditions, mannitol behaves like C(9)2Na. These data indicate that HO. scavenging capacity of C(9)2Na in vitro, and represent a useful tool for further investigations on the mechanisms of action of azelaic acid in biological systems.
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PMID:Scavenging activity of azelaic acid on hydroxyl radicals "in vitro". 164 75

With the help of nanocrystalline TiO2, the direct electrochemistry of xanthine oxidase (XOD) was achieved and two pairs of redox waves were observed. The interaction between XOD and nitric oxide (NO) was also investigated. The experimental results reveal that NO can be reduced at a XOD-nano TiO2 film modified electrode. When the NO concentration was low, the reduced product, HNO, would inactivate the protein. However, when the NO concentration was high, HNO would continue to react with NO to form N2O2- and N3O3-, which would not inhibit XOD, and thus the amount of active protein did not decrease any further.
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PMID:Electrochemistry of xanthine oxidase and its interaction with nitric oxide. 1651 35