Rat liver DT-diaphorase as a nitroso-reductase.

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Properties and reaction mechanism of DT diaphorase from rat liver.

DT diaphorase was purified to homogeneity from rat liver and characterized. The molecular weight of the enzyme was calculated to be 5.0 h 0.06 x lo4 from sedimentation equilibrium experiments and to be 4.8 x IO4 by thin layer gel filtration method using Sephadex G-200. The identity of FAD as a prosthetic group was confirmed by o-amino acid oxidase test. It was found that 1 mole of FAD was prese...

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Prooxidant cytotoxicity of chromate in mammalian cells: the opposite roles of DT-diaphorase and glutathione reductase.

The geno- and cytotoxicity of chromate, an important environmental pollutant, is partly attributed to the flavoenzyme-catalyzed reduction with the concomitant formation of reactive oxygen species. The aim of this work was to characterize the role of NAD(P)H:quinone oxidoreductase (NQO1, DT-diaphorase, EC 1.6.99.2) and glutathione reductase (GR, EC 1.6.4.2) in the mammalian cell cytotoxicity of ...

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Prominent role of DT-diaphorase as a cellular mechanism reducing chromium(VI) and reverting its mutagenicity.

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Expression of DT-diaphorase and cytochrome P450 reductase correlates with mitomycin C activity in human bladder tumors.

Mitomycin C (MMC) is activated by DT-diaphorase (DTD) and cytochrome P450 reductase (P450R). In cancer cell lines, MMC cytotoxicity is correlated with DTD and P450R expression levels. The present study investigated the relationship between enzyme expression/activity and MMC cytotoxicity in patient bladder tumors. DTD and P450R expression was detected by competitive reverse transcription-PCR and...

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Crystal structure of rat liver dihydropteridine reductase.

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ژورنال

عنوان ژورنال: Chemical and Pharmaceutical Bulletin

سال: 1990

ISSN: 0009-2363,1347-5223

DOI: 10.1248/cpb.38.1096