Results 111 to 120 of about 1,029 (146)

Chemical Properties of Quinol Phosphate Esters and Inhibition of Alcohol Dehydrogenase by Them [PDF]

, 1975
Some phosphate and phosphorothiolate esters of hydroquinone and related phenols and thiophenols were prepared. Quinol phosphates were stable to alkaline hydrolysis but susceptible to oxidation. They inhibited yeast alcohol dehydrogenase probably owing to
江藤, 守総, 前川, 一之, 橋本, 恭明, Maekawa, Kazuyuki, Hashimoto, Yasuaki, Eto, Morifusa   +5 more
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Covalent modification of lactate dehydrogenase and alcohol dehydrogenase by alkannin derivatives [PDF]

, 2001
Covalent modification of four isolated alkannin derivatives (alkannin, acetylalkannin, beta, beta -dimethylacrylalkannin and beta -acetoxyisovalerylalkannin, respectively) on rabbit muscle latate dehydrogenase (LDHase) and yeast Alcohol Dehydrogenase ...
Huang, ZS, Che, ZT, Ma, L., Gu, LQ, Duan, ZF   +4 more
core  

Effects of Silver and Mercurials on Yeast Alcohol Dehydrogenase

Journal of Biological Chemistry, 1960
P J, SNODGRASS, B L, VALLEE, F L, HOCH
openaire   +2 more sources

Chemical Properties of Quinol Phosphate Esters and Inhibition of Alcohol Dehydrogenase by Them [PDF]

Some phosphate and phosphorothiolate esters of hydroquinone and related phenols and thiophenols were prepared. Quinol phosphates were stable to alkaline hydrolysis but susceptible to oxidation. They inhibited yeast alcohol dehydrogenase probably owing to
江藤, 守総, 前川, 一之, 橋本, 恭明, Maekawa, Kazuyuki, Hashimoto, Yasuaki, Eto, Morifusa   +5 more
core  

Activity and kinetics studies of yeast alcohol dehydrogenase in a reverse micelle formulated from functional surfactants

Open Chemistry, 2009
Zhang Yun, Huang Xirong, Ji Guanglei, Li Ying, Liu Weifeng, Qu Yinbo   +5 more
doaj   +1 more source

CRYSTALLINE ALCOHOL DEHYDROGENASE FROM BAKERS' YEAST

Journal of Biological Chemistry, 1950
openaire   +2 more sources

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Yeast alcohol dehydrogenase II

Archives of Biochemistry and Biophysics, 1957
Abstract 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, 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
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources