Results 201 to 210 of about 14,865 (241)

Absence of xanthine oxidoreductase activity in human myocardium

Cardiovascular Research, 1991
The aim was to examine whether or not xanthine oxidase activity may be a significant source of oxygen derived free radicals in the human heart.Xanthine oxidoreductase activity of human myocardium was assayed in vitro. In addition, tests were performed to assess whether or not endogenous inhibitors of the enzyme were present in myocardial homogenates ...
T, Podzuweit, H, Beck, A, Müller, R, Bader, G, Görlach, H H, Scheld   +5 more
openaire   +4 more sources

Xanthine oxidoreductase and its inhibitors: relevance for gout

Clinical Science, 2016
Xanthine oxidoreductase (XOR) is the rate-limiting enzyme in purine catabolism and converts hypoxanthine to xanthine, and xanthine into uric acid. When concentrations of uric acid exceed its biochemical saturation point, crystals of uric acid, in the form of monosodium urate, emerge and can predispose an individual to gout, the commonest form of ...
Richard O, Day, Bishoy, Kamel, Diluk R W, Kannangara, Kenneth M, Williams, Garry G, Graham   +4 more
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Xanthine Oxidoreductase Activities

2020
Xanthine oxidoreductase (XOR) is the enzyme that catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid. XOR is widely distributed throughout living organisms and is highly conserved in prokaryotic, plant, and animal species. XOR activity is very versatile, generating both pro-oxidant (primarily within the cell) and anti-oxidant (
Letizia Polito, Maria Giulia Battelli, Massimo Bortolotti, Andrea Bolognesi   +3 more
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Structure and Function of Xanthine Oxidoreductase

ChemInform, 2006
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
openaire   +1 more source

Mechanism of Inhibition of Xanthine Oxidoreductase by Allopurinol: Crystal Structure of Reduced Bovine Milk Xanthine Oxidoreductase Bound with Oxipurinol

Nucleosides, Nucleotides and Nucleic Acids, 2008
Inhibitors of xanthine oxidoreductase block conversion of xanthine to uric acid and are therefore potentially useful for treatment of hyperuricemia or gout. We determined the crystal structure of reduced bovine milk xanthine oxidoreductase complexed with oxipurinol at 2.0 A resolution.
Ken, Okamoto, Bryan T, Eger, Tomoko, Nishino, Emil F, Pai, Takeshi, Nishino   +4 more
openaire   +2 more sources

[Inhibitors of xanthine oxidoreductase].

Nihon rinsho. Japanese journal of clinical medicine, 2008
Inhibitors of xanthine oxidoreductase decrease production of uric acid, thus they act as hypouricemic drugs. Allopurinol, a prototypical xanthine oxidoreductase inhibitor, has been widely prescribed for treatment of gout and hyperuricemia. However, severe side effects of allopurinol may occur in patients with renal insufficiency.
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Lower Xanthine Oxidoreductase Activity in Isolated Perfused Hearts if Xanthine Replaces Hypoxanthine as Substrate

1991
In normal cardiac tissue xanthine oxidoreductase is present in the dehydrogenase form. During ischemia xanthine dehydrogenase is converted to xanthine oxidase, which generates free radicals during reperfusion. Both forms catalyze the breakdown of hypoxanthine to xanthine and xanthine to urate.
M, Janssen, J W, de Jong, A S, Nieukoop, E, Keijzer   +3 more
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Xanthine oxidoreductase: dehydrogenase to oxidase conversion

Biochemical Society Transactions, 1997
M G, Ryan, A, Balendran, R, Harrison, A, Wolstenholme, G B, Bulkley   +4 more
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HISTORY OF MILK XANTHINE OXIDOREDUCTASE

Biochemical Society Transactions, 1997
V. MASSEY, C. H. HARRIS
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Xanthine oxidoreductase. Biochemical, biological and pathogenic functions.

Sbornik lekarsky, 1996
Primary biochemical role of xanthine oxidoreductase (XOR, EC 1.1.1.204 and EC 1.1.3.22.) is the hydroxylation of hypoxathine and xanthine to form uric acid. This enzyme may produce very reactive oxygen forms which can be pathogenic. Although it is one of the longest known and most continuously studied enzymes, its biological function remains unclear ...
S, Stipek, L, Novak, J, Crkovska, T, Zima, J, Platenik   +4 more
openaire   +1 more source