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חיפוש מתקדם
Plant and Cell Physiology
Fuchs, Y., Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, Israel
Gertman, E., Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, Israel
The temperature at which incubation with ethylene takes place has a significant effect on the purified alcohol dehydrogenase (ADH) activity subsequently determined at room temperature. Ethylene can be separated completely from ADH on a Sephadex column. Factors, such as the ionic strength of the buffer and the presence of gelatin and NAD during the incubation with ethylene can modify the effects of the gas. In yeast cells the effects of ethylene on ADH activity are similar to those in the purified system. The presence of cyloheximide in the incubation medium did not suppress the effects of ethylene on ADH activity. Ethylene may induce its effect, directly, through involvement in hydrophobic bonding in enzymes. © 1974 Oxford University Press.
פותח על ידי קלירמאש פתרונות בע"מ -
הספר "אוצר וולקני"
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תנאי שימוש
Studies of the effects of ethylene on yeast alcohol dehydrogenase activity
15
Fuchs, Y., Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, Israel
Gertman, E., Agricultural Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, Israel
Studies of the effects of ethylene on yeast alcohol dehydrogenase activity
The temperature at which incubation with ethylene takes place has a significant effect on the purified alcohol dehydrogenase (ADH) activity subsequently determined at room temperature. Ethylene can be separated completely from ADH on a Sephadex column. Factors, such as the ionic strength of the buffer and the presence of gelatin and NAD during the incubation with ethylene can modify the effects of the gas. In yeast cells the effects of ethylene on ADH activity are similar to those in the purified system. The presence of cyloheximide in the incubation medium did not suppress the effects of ethylene on ADH activity. Ethylene may induce its effect, directly, through involvement in hydrophobic bonding in enzymes. © 1974 Oxford University Press.
Scientific Publication
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