Results 211 to 220 of about 25,198 (259)
Some of the next articles are maybe not open access.
Yeast alcohol dehydrogenase II
Archives of Biochemistry and Biophysics, 1957Abstract Many lines of evidence support the existence of a new alcohol dehydrogenase in yeast. The new enzyme showed a broad spectrum of activity with various alcohols, ethanol having the highest activity. Its properties in many respects appear to be different from the classical alcohol dehydrogenase, and the new enzyme is more able to oxidize the ...
K, EBISUZAKI, E S, GUZMAN BARRON
openaire +2 more sources
Rapid purification of yeast alcohol dehydrogenase
Analytical Biochemistry, 1981Abstract 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 +2 more
openaire +2 more sources
Inhibition of yeast alcohol dehydrogenase by dehydroretronecine
Food and Cosmetics Toxicology, 1977Abstract 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 +3 more
openaire +2 more sources
Inactivation of Yeast Alcohol Dehydrogenase by Nitrilopropionamides
Journal of Enzyme Inhibition and Medicinal Chemistry, 1994A series of halonitrilopropionamides have been examined as potential inhibitors of yeast alcohol dehydrogenase. Analogues with a good leaving group on the alpha-carbon, and a geminal electronegative atom, were found to be initial competitive inhibitors against NAD with inhibition constants as low as 0.6 microM.
Ronald E Viola
exaly +3 more sources
Interaction of Eu3+ with Yeast Alcohol Dehydrogenase
Journal of Protein Chemistry, 1999The 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
openaire +2 more sources
Adventitious inhibition of yeast alcohol dehydrogenase
Archives of Biochemistry and Biophysics, 1960Abstract 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 +3 more
openaire +2 more sources
The zinc content of yeast alcohol dehydrogenase
Biochemical and Biophysical Research Communications, 1976Abstract Analyses for zinc in high specific activity preparations of yeast alcohol dehydrogenase (YADH) indicate a metal content of 1.8–1.9 moles of zinc per mole of enzyme subunit. This zinc content is observed for YADH prepared from Bakers yeast by recrystallization from Am2SO4 containing 1 mM EDTA, followed by chromatography on DE-52 and Sephadex ...
J P, Klinman, K, Welsh
openaire +2 more sources
Multiple inhibition of yeast alcohol dehydrogenase
Archives of Biochemistry and Biophysics, 1965Abstract Multiple inhibition of the yeast alcohol dehydrogenase-catalyzed oxidation of ethanol was investigated; four different inhibitors were used that were known to function competitively with respect to NAD + in these reactions. The inhibitors, adenosine diphosphate ribose, adenosine diphosphate, N 1 -methylnicotinamide chloride, and 1,10 ...
B M, Anderson, M L, Reynolds
openaire +2 more sources
Catalysis by Yeast Alcohol Dehydrogenase
1990Table 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 +6 more
openaire +2 more sources