Results 201 to 210 of about 623,332 (218)
Some of the next articles are maybe not open access.
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 2002
Inbred strains of mice remain a valuable resource for genetic dissection of complex traits including responses to drugs and chemicals, particularly alcohol. As a novel source of candidate genes for further analysis, we have used mRNA differential displays to identify genes with differential expression in the brains of ethanol-preferring (C57BL/6J) vs ...
Michelle, Harrison, Shiva M, Singh
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Inbred strains of mice remain a valuable resource for genetic dissection of complex traits including responses to drugs and chemicals, particularly alcohol. As a novel source of candidate genes for further analysis, we have used mRNA differential displays to identify genes with differential expression in the brains of ethanol-preferring (C57BL/6J) vs ...
Michelle, Harrison, Shiva M, Singh
openaire +2 more sources
Substrate specificity of citrus alcohol: NAD oxidoreductase
Journal of Agricultural and Food Chemistry, 1971Joseph H. Bruemmer, Bongwoo. Roe
openaire +1 more source
Generation of Oxidoreductases with Dual Alcohol Dehydrogenase and Amine Dehydrogenase Activity
Chemistry - A European Journal, 2021Vasilis Tseliou +2 more
exaly
Immobilization as a Strategy for Improving Enzyme Properties-Application to Oxidoreductases
Molecules, 2014Urszula Guzik +2 more
exaly
Review of NAD(P)H-dependent oxidoreductases: Properties, engineering and application
Biochimica Et Biophysica Acta - Proteins and Proteomics, 2018John Heap +2 more
exaly
Alcohol as a Primary Risk Factor in Oral Squamous Carcinoma
Ca-A Cancer Journal for Clinicians, 1981A Mashberg, L Garfinkel
exaly