نتایج جستجو برای: alcohol dehydrogenase

تعداد نتایج: 183235  

Journal: :Journal of molecular biology 1982
A M Gronenborn G M Clore

The glycosidic bond torsion angles and the conformations of the two riboses of NAD’ bound to yeast and horse liver alcohol dehydrogenase in solution have been determined by a novel method involving the measurement of proton-proton transferred nuclear Overhauser enhancements by ‘H-nuclear magnetic resonance. In both cases the conformation of the-a8eirosine and nicotinamide ribose is 3’-endo of t...

Journal: :The Journal of biological chemistry 1961
R D ZACHMAN J A OLSON

Retinene reductase, an enzyme which catalyzes the diphosphopyridine nucleotide-dependent reduction of vitamin A aldehyde (retinene) to vitamin A alcohol, was first demonstrated with homogenates of frog and cattle retinas (1, 2). Because crude rabbit liver extracts (3) and crystalline horse liver alcohol dehydrogenase (4) catalyze the oxidation of vitamin A into retinene, the general involvement...

2009
KEITH F. TIPTON

Affinity precipitation with N,, N,'-adipodihydrazido-bis( N6-carboxymethyl-NAD+) (bis-NAD+) as a means of isolating alcohol dehydrogenase (EC 1.1.1.1) and lactate dehydrogenase (EC 1.1.1.27) has already been reported (Flygare et al., 1983; Beattie et al., 1984). However, affinity precipitation of alcohol dehydrogenase in the presence of bis-NAD+ and pyrazole has been found to give mixed results...

1997
Jiulin Xia Kevin Mattison Vincent Romano Paul L. Dubin Barry B. Muhoberac

Complexation of alcohol dehydrogenase (ADH) and trypsin with poly(diallyldimethyl-ammonium chloride) (PDADMAC) in dilute electrolyte solution was studied by turbidimetric titration, quasi-elastic light scattering (QELS), and electrophoretic light scattering (ELS). Both QELS and turbidimetric titration show that PDADMAC forms complexes with ADH and trypsin in 0.01M NaCl solution at pH ¢ 6.8 and ...

Journal: :Genetics 1978
J P Thirion B Talbot

Alcohol dehydrogenase (alcohol: NAD oxidoreductase, E.C. 1.1.1.1.) mutants of Chinese hamster somatic cells were isolated as resistant to allyl alcohol (ALLR). The ALLR phenotypes of the mutant clones were reproducible with high fidelity and stable over long intervals of growth in the absence of the selecting drug. Several mutants, Adh-1, Adh-2, Adh-9 and Adh-13, resistant to allyl alcohol were...

Journal: :Biochemical Society transactions 1977
J H Walker R J Mayer

We have also examined similar parameters for several other enzymes; the trend suggests that in these cases there is a correlation between apparent association constant and capacity. These enzymes include yeast glutathione reductase, glucose 6-phosphate dehydrogenase, glutamate dehydrogenase, alcohol dehydrogenase and malate dehydrogenase, Neurospora crassa glutamate dehydrogenase, pig heart iso...

Journal: :Bioscience, biotechnology, and biochemistry 2006
Yuji Tasaki Hiromichi Yoshikawa Hiroto Tamura

Octylphenol polyethoxylate (OPEO(n)) biodegradation by Pseudomonas putida S-5 under aerobic conditions is initiated by the oxidation of its terminal alcohol group by alcohol dehydrogenase. A DNA fragment, containing an alcohol dehydrogenase gene (adh1), was isolated using a combination of degenerate PCR and inverse PCR. The predicted translation product of adh1 showed significant sequence simil...

Journal: :The Journal of biological chemistry 1971
J M Yound J H Wang

Two classes of metal ion binding sites in horse liver alcohol dehydrogenase are distinguished by the observed rates of replacement of zinc by cobalt in acetate and in Z-(N-morpholine)-ethane sulfonic acid buffers. Hybrid enzymes containing both zinc and cobalt metal ions have been prepared and exhibit visible absorption maxima at 655 nm and 740 nm. Binding of azide, a substrate-competitive inhi...

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