Results 231 to 240 of about 34,724 (282)

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, J W, De Jong, E, Harmsen, P P, De Tombe, P W, Achterberg   +4 more
openaire   +2 more sources

Catalytic Electrochemistry of Xanthine Dehydrogenase

The Journal of Physical Chemistry B, 2012
We report the mediated electrocatalytic voltammetry of the molybdoenzyme xanthine dehydrogenase (XDH) from Rhodobacter capsulatus at a thiol-modified Au electrode. The 2-electron acceptor N-methylphenazinium methanesulfonate (phenazine methosulfate, PMS) is an effective artificial electron transfer partner for XDH instead of its native electron ...
Kalimuthu, Palraj, Leimkuehler, Silke, Bernhardt, Paul V.   +2 more
openaire   +4 more sources

Liver xanthine dehydrogenase and iron mobilization

Biochemical and Biophysical Research Communications, 1982
Abstract Administration of a tungsten-supplemented diet to young rats for 10 weeks resulted in an 80% – 90% reduction in the liver xanthine dehydrogenase activity and a 100% increase in the liver non-heme iron content as compared to control animals. A time course study of the effect of dietary tungsten in adult rats demonstrated that an increase in ...
R W, Topham, M C, Walker, M P, Calisch
openaire   +2 more sources

Xanthine dehydrogenase in bovine blood serum

Experientia, 1956
Le serum sanguin des bovides contient des quantites elevees de xanthine dehydrogenase. On l'a demontre par le dosage de l'acide urique et la reduction du triphenyltetrazolium apres incubation avec de la xanthine. Des experiences complementaires faites avec differents inhibiteurs de la xanthine oxidase et la preparation d'une fraction active donnant le ...
O R, AFFONSO, E, MITIDIERI, G G, VILLELA
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, Y, Moriwaki, S, Takahashi, M, Suda, K, Higashino   +4 more
openaire   +2 more sources

Regulation of xanthine dehydrogenase and xanthine oxidase activity by hypoxia

American Journal of Physiology-Lung Cellular and Molecular Physiology, 1996
The present study determined the effect of hypoxia on xanthine dehydrogenase (XDH) and xanthine oxidase (XO) activity and gene and protein expression in cultured bovine aortic endothelial cells (BAEC). BAEC were exposed to hypoxia (3% O2) or anoxia (0% O2) for 24 or 48 h and to 24 h of hypoxia followed by 24 h of reoxygenation.
W B, Poss, T P, Huecksteadt, P C, Panus, B A, Freeman, J R, Hoidal   +4 more
openaire   +2 more sources

[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
openaire   +1 more source

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, B A, Blakistone, H E, Swaisgood, H R, Horton   +3 more
openaire   +2 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.
openaire   +2 more sources