Results 221 to 230 of about 104,574 (275)

Adventitious inhibition of yeast alcohol dehydrogenase

Archives of Biochemistry and Biophysics, 1960
Abstract The inhibition of yeast alcohol dehydrogenase by N′ -methylnicotinamide has been shown to be due to contaminating silver ions present in commercial preparations of this reagent. Contamination by metal ions, which was assessed by quantitative analysis, also accounts for the inhibition of yeast alcohol dehydrogenase by semicarbazide ...
F L, HOCH, R G, MARTIN, W E, WACKER, B L, VALLEE   +3 more
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Rapid purification of yeast alcohol dehydrogenase

Analytical Biochemistry, 1981
Abstract Making use of the unusual stability of yeast alcohol dehydrogenase in the presence of ethanol, a simple, rapid procedure for isolating this enzyme in high yield is presented. Once-crystallized enzyme is obtained within 5 h of commencing the procedure; this is undegraded and substantially free of proteolytic activity.
R K, Scopes, K, Griffiths-Smith, D G, Millar   +2 more
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Surface functionalization of chitosan-coated magnetic nanoparticles for covalent immobilization of yeast alcohol dehydrogenase from Saccharomyces cerevisiae

Journal of Magnetism and Magnetic Materials, 2010
Gui-yin Li, Zhide Zhou, Yuan‐jian Li, Ke‐long Huang, M. Zhong   +4 more
semanticscholar   +3 more sources

Catalysis by Yeast Alcohol Dehydrogenase

1990
Table 7 presents a brief summary of the effects of various mutations on some of the relevant kinetic constants. The results illustrate several important features of the use of site-directed mutagenesis in exploring structure and function of enzymes. Note that most of the mutations affect a given step or kinetic parameter in the mechanism, such as the ...
B V, Plapp, A J, Ganzhorn, R M, Gould, D W, Green, T, Jacobi, E, Warth, D A, Kratzer   +6 more
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Inhibition of yeast alcohol dehydrogenase by dehydroretronecine

Food and Cosmetics Toxicology, 1977
Abstract The interaction of dehydroretronecine, a hepatocarcinogenic metabolite of the pyrrolizidine alkaloid monocrotaline, with yeast alcohol dehydrogenase (ADH), cysteine and bovine serum albumin (BSA) was studied. Dehydroretronecine inhibited ADH with an inhibition constant (Ki) of 3.38 × 10−2 m at pH 7.5 and 25 °C.
P S, Sun, M T, Hsia, F S, Chu, J R, Allen   +3 more
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Zinc Release from Irradiated Yeast Alcohol Dehydrogenase

International Journal of Radiation Biology and Related Studies in Physics, Chemistry and Medicine, 1987
The release of Zn2+ from gamma-irradiated yeast alcohol dehydrogenase has been measured using atomic absorption spectrometry. Radiolysis is accompanied by release of Zn2+ at a rate which is dependent on the nature of the free radicals available for reaction. Hydroxyl radicals and hydrogen atoms readily cause zinc release with G values of 0.13 and 0.11 (
S, Abelidis, J S, Moore, A, Chakravarty
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Functional Mutants of Yeast Alcohol Dehydrogenase

1982
Selection of petite strains of yeast (that is, strains unable to respire aerobically) on media containing allyl alcohol will result in enrichment for mutants at the ADC1 locus. This locus codes for the constitutive alcohol dehydrogenase, ADH-I, which is primarily responsible for the production of ethanol in yeast. The mutant enzymes are functional, and
C, Wills, P, Kratofil, T, Martin
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Interaction of Eu3+ with Yeast Alcohol Dehydrogenase

Journal of Protein Chemistry, 1999
The activity of yeast alcohol dehydrogenase is markedly enhanced by Eu3+ ions. At pH 7.0 two binding constants for Eu3+, 1.0x10(-2) and 2.0x10(-3) microM, were obtained using a Scatchard plot. The presence of Zn2+ ions restricts the Eu3+ -induced increase in the activity of yeast alcohol dehydrogenase.
Y X, Zhang, C L, Duan, H M, Zhou
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Nitrogen base inhibition of yeast alcohol dehydrogenase

Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1966
Summary The oxidation of ethanol as catalyzed by yeast alcohol dehydrogenase (alcohol: NAD + oxidoreductase, EC 1.1.1.1) is inhibited by a variety of nitrogen bases. Inhibition by 2,9-dimethyl-1,10-phenanthroline, 1,5-phenanthroline, 5,6-benzoquinoline, 7,8-benzoquinoline, quinoline and adenosine was in each case shown to be competitive with respect
B M, Anderson, M L, Reynolds, C D, Anderson   +2 more
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Coenzyme binding capacity of yeast alcohol dehydrogenase

Biochemical and Biophysical Research Communications, 1978
Abstract Commercial lyophilized preparations of yeast alcohol dehydrogenase from Boehringer G.m.b.H. (Mannheim, Germany) bind 2 mols of reduced coenzyme/144000 g of enzyme (1). After the purification by a DEAE-Sephadex column chromatography, the coenzyme binding capacity is raised to 4 mols of NADH/mol of enzyme.
V, Leskovac, D, Pericin
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