Results 201 to 210 of about 16,608 (226)
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Journal of Liquid Chromatography, 1979
Abstract Nicotinamide adenine dinucleotide (NAD) is an important cofactor in a number of oxidoreductase enzyme systems. The detection and quantitation of its reduced form (NADH) is the basis for a number of methods which determine both substrates and enzyme activity.
Gregory C. Davis +2 more
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Abstract Nicotinamide adenine dinucleotide (NAD) is an important cofactor in a number of oxidoreductase enzyme systems. The detection and quantitation of its reduced form (NADH) is the basis for a number of methods which determine both substrates and enzyme activity.
Gregory C. Davis +2 more
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Biochemical and Biophysical Research Communications, 2012
Alcohol dehydrogenases (ADHs) from thermophilic microorganisms are interesting enzymes that have their potential applications in biotechnology and potentially provide insight into the mechanisms of action of thermo-tolerant proteins. The molecular mechanisms of ADHs under thermal stress in vivo have yet to be explored.
Qian, Wang +7 more
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Alcohol dehydrogenases (ADHs) from thermophilic microorganisms are interesting enzymes that have their potential applications in biotechnology and potentially provide insight into the mechanisms of action of thermo-tolerant proteins. The molecular mechanisms of ADHs under thermal stress in vivo have yet to be explored.
Qian, Wang +7 more
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The Analyst, 1987
Bacterial luciferase and oxidoreductase extracted from Vibrio harveyi were co-immobilised on cyanogen bromide-activated Sepharose 4B and used in a flow injection manifold for the rapid and sensitive determination of ethanol and alcohol dehydrogenase. The detection limits were 30 pmol for ethanol and 0.03 pmol for alcohol dehydrogenase.
A, Nabi, P J, Worsfold
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Bacterial luciferase and oxidoreductase extracted from Vibrio harveyi were co-immobilised on cyanogen bromide-activated Sepharose 4B and used in a flow injection manifold for the rapid and sensitive determination of ethanol and alcohol dehydrogenase. The detection limits were 30 pmol for ethanol and 0.03 pmol for alcohol dehydrogenase.
A, Nabi, P J, Worsfold
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Process Biochemistry, 2011
Abstract The stereoinversion process involving two sequential stereoselective oxidation and reduction reactions by oxidoreductases was a typical and important one-pot method for chiral secondary alcohol synthesis which has great potential for industrial application.
Xiao Qing Mu +3 more
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Abstract The stereoinversion process involving two sequential stereoselective oxidation and reduction reactions by oxidoreductases was a typical and important one-pot method for chiral secondary alcohol synthesis which has great potential for industrial application.
Xiao Qing Mu +3 more
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Journal of biochemistry, 1991
Acyclic monoterpene primary alcohol:NADP+ oxidoreductase, a key enzyme in the biosynthesis of monoterpene alcohols in plants, is unstable and has been only poorly characterized. However we have established conditions which stabilize the enzyme from Rauwolfia serpentina cells, and then purified it to homogeneity.
H, Ikeda +6 more
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Acyclic monoterpene primary alcohol:NADP+ oxidoreductase, a key enzyme in the biosynthesis of monoterpene alcohols in plants, is unstable and has been only poorly characterized. However we have established conditions which stabilize the enzyme from Rauwolfia serpentina cells, and then purified it to homogeneity.
H, Ikeda +6 more
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The FEBS Journal, 2010
The in vitro Entamoeba histolytica pyruvate:ferredoxin oxidoreductase (EhPFOR) kinetic properties and the effect of oxidative stress on glycolytic pathway enzymes and fluxes in live trophozoites were evaluated. EhPFOR showed a strong preference for pyruvate as substrate over other oxoacids.
Erika, Pineda +5 more
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The in vitro Entamoeba histolytica pyruvate:ferredoxin oxidoreductase (EhPFOR) kinetic properties and the effect of oxidative stress on glycolytic pathway enzymes and fluxes in live trophozoites were evaluated. EhPFOR showed a strong preference for pyruvate as substrate over other oxoacids.
Erika, Pineda +5 more
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International Journal of Cancer, 1990
AbstractNAD(P)H:(quinone‐acceptor)oxidoreductase (QAO), previously known as DT‐diaphorase, catalyzes the reduction of qui‐nones to hydroquinones. Enhanced activity of the enzyme has been suggested to protect cells against the cellular toxicity and carcinogenicity of quinones, but may activate some cyto‐toxic anti‐tumor quinones. Cytosolic levels of QAO,
J J, Schlager, G, Powis
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AbstractNAD(P)H:(quinone‐acceptor)oxidoreductase (QAO), previously known as DT‐diaphorase, catalyzes the reduction of qui‐nones to hydroquinones. Enhanced activity of the enzyme has been suggested to protect cells against the cellular toxicity and carcinogenicity of quinones, but may activate some cyto‐toxic anti‐tumor quinones. Cytosolic levels of QAO,
J J, Schlager, G, Powis
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Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis, 2006
Colorectal cancer (CRC) is one of the most common forms of cancer in Western countries. CRC has been associated with genetic and lifestyle factors. Individual susceptibility to CRC may be due partly to variations in detoxification capacity in the gastrointestinal tract.
Logt, E.M.J. van der +7 more
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Colorectal cancer (CRC) is one of the most common forms of cancer in Western countries. CRC has been associated with genetic and lifestyle factors. Individual susceptibility to CRC may be due partly to variations in detoxification capacity in the gastrointestinal tract.
Logt, E.M.J. van der +7 more
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Substrate specificity of citrus alcohol: NAD oxidoreductase
Journal of Agricultural and Food Chemistry, 1971Joseph H. Bruemmer, Bongwoo. Roe
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Generation of Oxidoreductases with Dual Alcohol Dehydrogenase and Amine Dehydrogenase Activity
Chemistry - A European Journal, 2021Vasilis Tseliou +2 more
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