Results 121 to 130 of about 169,173 (169)
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Xanthine oxidase and xanthine dehydrogenase

The FASEB Journal, 1995
Xanthine oxidase and xanthine dehy‐drogenase are enzymes involved in the metabolism of purines and pyrimidines in various organisms. Their relationship to one another has been the subject of considerable debate, primarily because of their proposed roles in ischemia/reperfasion damage in tissues.
Russ Hille, Takeshi Nishino
openaire   +1 more source

Myocardial xanthine oxidase/dehydrogenase

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1983
High-energy phosphates in heart muscle deprived of oxygen are rapidly broken down to purine nucleosides and oxypurines. We studied the role of xanthine oxidase/dehydrogenase (EC 1.2.3.2/EC 1.2.1.37) in this process with novel high-pressure liquid chromatographic techniques.
B, Schoutsen   +4 more
openaire   +2 more sources

Ethanol as a xanthine dehydrogenase inhibitor

Metabolism, 1995
In the present study, we investigated whether ethanol inhibits the activity of xanthine dehydrogenase. Ethanol and/or inosine were administered to normal subjects, and plasma concentration and urinary excretion of purine bases were measured together with blood concentrations of lactic acid and pyruvic acid.
T, Yamamoto   +4 more
openaire   +2 more sources

Mammalian Xanthine Oxidoreductase – Mechanism of Transition From Xanthine Dehydrogenase to Xanthine Oxidase

FEBS Journal, 2008
Reactive oxygen species are generated by various biological systems, including NADPH oxidases, xanthine oxidoreductase, and mitochondrial respiratory enzymes, and contribute to many physiological and pathological phenomena. Mammalian xanthine dehydrogenase (XDH) can be converted to xanthine oxidase (XO), which produces both superoxide anion and ...
Emil F. Pai   +2 more
exaly   +3 more sources

Xanthine dehydrogenase of chicken liver

Biochimica et Biophysica Acta, 1955
Xanthine dehydrogenase of chicken liver is shown to reduce DPN nearly as fast as it reduces methylene blue. Strong evidence is produced showing that DPN is the in vivo acceptor for this enzyme and comparisons with milk xanthine oxidase are made. Other properties of the enzyme are described.
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[Xanthine oxidase (xanthine dehydrogenase)].

Nihon rinsho. Japanese journal of clinical medicine, 1997
Xanthine oxidase (xanthine dehydrogenase) is composed of two identical subunits of approximately 150,000 daltons. Each subunit contains four oxdation-reduction active cofactors/monomers. In vivo, the enzyme exists mostly as the dehydrogenase type (the NAD-dependent type).
S, Sumi, Y, Wada
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Occurrence of Xanthine Dehydrogenase in Chlamydomonas reinhardii: A Common Cofactor Shared by Xanthine Dehydrogenase and Nitrate Reductase

Planta, 1981
Wild-type Chlamydomonas reinhardii cells have xanthine dehydrogenase activity when grown with nitrate, nitrite, urea, or amino acid media. Mutant strains 102, 104, and 307 of Chlamydomonas, lacking both xanthine dehydrogenase and nitrate reductase activities, were incapable of restoring the NADPH-nitrate reductase activity of the mutant nit-1 of ...
J Cárdenas
exaly   +3 more sources

The Mechanism of Conversion of Xanthine Dehydrogenase to Xanthine Oxidase

1998
Xanthine dehydrogenase and xanthine oxidase are complex metalloflavoproteins that represent alternate forms of the same gene product. The cDNAs encoding the enzymes have been cloned from several sources, and structural information is becoming available.
Takeshi Nishino   +4 more
openaire   +1 more source

Inhibitory action of quercetin on xanthine oxidase and xanthine dehydrogenase activity

Pharmacological Research Communications, 1985
Quercetin is an equally good inhibitor of xanthine oxidase (type O, oxygen-reducing enzyme) and xanthine dehydrogenase (type D, NAD+-reducing enzyme) activity of a preparation of the xanthine-oxidizing enzyme partially purified from rat liver. The inhibition seems competitive with the oxidase form and non-competitive (mixed-type) with the dehydrogenase
A, Bindoli, M, Valente, L, Cavallini
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Sulfhydryl oxidase-catalyzed conversion of xanthine dehydrogenase to xanthine oxidase

Archives of Biochemistry and Biophysics, 1981
Abstract Xanthine oxidase may be isolated from various mammalian tissues as one of two interconvertible forms, viz., a dehydrogenase (NAD+ dependent, form D) or an oxidase (O2 utilizing, form O). A crude preparation of rat liver xanthine dehydrogenase (form D) was treated with an immobilized preparation of crude bovine sulfhydryl oxidase.
D A, Clare   +3 more
openaire   +2 more sources

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