Results 231 to 240 of about 25,198 (259)
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Coenzyme binding capacity of yeast alcohol dehydrogenase
Biochemical and Biophysical Research Communications, 1978Abstract 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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Inhibition of yeast alcohol dehydrogenase by alkylammonium chlorides
Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1965Abstract Five alkylammonium chlorides were shown to be competitive inhibitors with respect to NAD + in the yeast alcohol dehydrogenase (alcohol:NAD + oxidoreductase, EC 1.1.1.1)-catalyzed oxidation of ethanol. This inhibition increases with increasing chain length of the alkyl substituents of these compounds and is consistent with a hydrophobic ...
B M, ANDERSON, M L, REYNOLDS
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Production of yeast alcohol dehydrogenase isoenzymes by selection
Nature, 1976Mutants of yeast alcohol dehydrogenase have been produced that protect the cell against the poisonous aldehyde acrolein by increasing the NADH-NAD ratio. The altered properties include changes both in binding constants and in cooperativity. Such mutants may be useful in exploring the nature of adaptation at the molecular level.
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A Kinetic Study of Yeast Alcohol Dehydrogenase
Journal of Chemical Education, 1994A system that is more challenging than the single-substrate case and has only "visible" substrates is the yeast alcohol dehydrogenase system in which the enzyme has two substrates - ethanol and NAD+ - both of which can be easily varied.
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Regulation of Yeast Alcohol Dehydrogenase Isozymes
1981The two major alcohol dehydrogenases of yeast are coded by separate nuclear genes, and show 95% amino acid homology. Nonetheless, the “constitutive” ADH, ADH-I, preferentially catalyzes the reaction acetaldehyde → ethanol, and the inducible ADH, ADH-II, preferentially catalyzes the reverse reaction.
Christopher Wills +2 more
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The inhibition of yeast alcohol dehydrogenase by borate
Biochimica et Biophysica Acta, 1961A H, ROUSH, B B, GOWDY
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Mechanism of Action of Yeast Alcohol Dehydrogenase
Nature, 1962B R, RABIN, E P, WHITEHEAD
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INACTIVATION OF YEAST ALCOHOL DEHYDROGENASE BY ULTRAVIOLET LIGHT
Photochemistry and Photobiology, 1968Dose, K., Krause, G.
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