Results 141 to 150 of about 17,774 (187)

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
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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
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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
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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
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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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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, Ken Okamoto, Shigeko Nakanishi, Hiroyuki Hori, Tomoko Nishino   +4 more
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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, B A, Blakistone, H E, Swaisgood, H R, Horton   +3 more
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Regulation of the Kidney Xanthine Dehydrogenase by Glutaminase

Archives Internationales de Physiologie et de Biochimie, 1979
The steady-state concentrations of glutamine, glutamate and ammonia in the kidney cells might regulate the rate of renal xanthine dehydrogenase activity. Both glutamate and glutamine were found to be effective inhibitors of the renal xanthine dehydrogenase activity in vivo. The inhibition by glutamate depends essentially on the glutaminase inhibition.
O R, Affonso, L J, Santos, E, Mitidieri
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