Alcohol dehydrogenase activity in Rhodotorula glutinis

1973 ◽  
Vol 19 (3) ◽  
pp. 353-358 ◽  
Author(s):  
Casimir J. Woscinski ◽  
Dan O. McClary
Keyword(s):  
Alcohol Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Rhodotorula Glutinis ◽  
Cinnamyl Alcohol Dehydrogenase ◽  
Cinnamyl Alcohol ◽  
Glucose Medium ◽  
Whole Cells ◽  
Alcohol Dehydrogenase Activity ◽  
Ethanol Medium ◽  
Significant Difference

Whole-cell extracts of Rhodotorula glutinis grown on yeast extract – glucose medium contained minute quantities of NAD-dependent alcohol dehydrogenase and cinnamyl alcohol dehydrogenase. Significantly greater quantities of these enzymes, as well as an NADP-dependent alcohol dehydrogenase were contained by cells grown on the same medium with ethanol substituted for glucose as the growth substrate. Although the [Formula: see text] on ethanol of whole cells grown in ethanol medium was more than triple that of cells grown in glucose medium, there was no significant difference in the [Formula: see text] on glucose of whole cells grown in glucose or in ethanol medium. Thermal inactivation studies revealed that the NADP-dependent alcohol dehydrogenase was relatively heat-stable as compared with the NAD-dependent alcohol dehydrogenase. Gel column electrophoresis revealed three active bands of alcohol dehydrogenase activity which were identified as NAD-dependent alcohol dehydrogenase, NADP-dependent alcohol dehydrogenase, and cinnamyl alcohol dehydrogenase. The NAD- and NADP-dependent enzymes, particularly the latter, were active on higher alcohols but not on methanol.

Relation between Hepatic Alcohol Dehydrogenase Activity and the Ascorbic Acid in Leucocytes of Patients with Liver Disease J. Dow

1975 ◽  
Vol 49 (6) ◽  
pp. 603-608
Author(s):  
J. Dow ◽  
N. Krasner ◽  
A. Goldberg
Keyword(s):  
Ascorbic Acid ◽  
Liver Disease ◽  
Alcohol Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Acid Content ◽  
Ascorbic Acid Content ◽  
Control Subjects ◽  
Alcohol Dehydrogenase Activity ◽  
Significant Difference ◽  
Heavy Drinkers

1. Hepatic alcohol dehydrogenase activity and leucocyte ascorbic acid content were measured in thirty-five patients with liver disease and in ten control subjects with duodenal ulcer. The patients with liver disease were divided into three groups consisting of non-drinkers, moderate drinkers and alcoholic/heavy drinkers. 2. There was no significant difference in hepatic alcohol dehydrogenase activity between the groups with liver disease, but all patients had less than half the hepatic alcohol dehydrogenase activity of the control subjects (P < 0·001). 3. The ascorbic acid in leucocytes was significantly lower in the alcoholic/heavy drinker group than that in the control subjects (P < 0·02) when the Student's t-test was applied, but no significant difference was found when the Mann—Whitney U-test was used. 4. A correlation coefficient of r = 0·77 (P < 0·001) was observed among the thirty-five patients with liver disease when hepatic alcohol dehydrogenase activity was compared with leucocyte ascorbic acid content. An insignificant correlation (r = 0·332) was found in the control subjects with no liver disease. 5. This comparison was also significant among non-drinkers with liver disease (r = 0·873; P < 0001), moderate drinkers (r = 0·739; P < 0·02) and alcoholic/heavy drinkers (r = 0·702; P < 0·005). 6. The addition of ascorbic acid in vitro (0·5–10 mmol/l) had no effect on the activity of alcohol dehydrogenase. 7. The relation between hepatic alcohol dehydrogenase activity and leucocyte ascorbic acid content is probably a consequence of liver disease, as opposed to any specific effect of ascorbic acid deficiency or alcohol consumption on alcohol dehydrogenase activity.

The effect of respiratory deficiency on the alcohol dehydrogenase activity of baker's yeast

1972 ◽  
Vol 18 (1) ◽  
pp. 23-28 ◽  
Author(s):  
H. M. C. Heick
Keyword(s):  
Alcohol Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Isocitrate Lyase ◽  
Heat Stability ◽  
Relative Activity ◽  
Wild Type ◽  
Respiratory Deficiency ◽  
Alcohol Dehydrogenase Activity ◽  
Ethanol Medium ◽  
Respiratory Deficient

The effects of respiratory deficiency on the level of NAD-dependent alcohol dehydrogenase activity were studied. Respiratory-deficient mutants produced by acriflavine, and wild-type cells grown on glucose in the presence of chloramphenicol had elevated alcohol dehydrogenase activities compared with the wild-type cells grown on glucose. The increased activity was a result of an increase in ADH-I. The respiratory-deficient mutants appeared unable to produce ADH-II or isocitrate lyase even after incubation of the cells in ethanol medium. However, this transfer to ethanol medium increased the level of ADH-I activity. The presence of chloramphenicol in the ethanol medium further increased the alcohol dehydrogenase activity of these mutants. The effect of chloramphenicol in the wild-type cultures depended on the time of its addition to the culture. If chloramphenicol was present during both the period of growth on glucose and in the ethanol medium, ADH-II activity did not appear. If the cultures were grown on glucose in the absence of chloramphenicol, allowing respiration to develop, the subsequent presence of chloramphenicol in fresh ethanol medium did not prevent the appearance of either ADH-II or isocitrate lyase activity. The respiratory-deficient mutants also contained alcohol dehydrogenase activity which resembles ADH-III in respect to electrophoretic mobility, heat stability, and relative activity with various alcohols as substrates.

Alcohol dehydrogenase activity in the yeast Saccharomyces fragilis

1972 ◽  
Vol 18 (1) ◽  
pp. 35-44 ◽  
Author(s):  
Roger Sanfaçon ◽  
Roger Rouillard ◽  
Micheline Goupil ◽  
H. M. C. Heick
Keyword(s):  
Oxygen Consumption ◽  
Alcohol Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Electrophoretic Pattern ◽  
Alcohol Oxidase ◽  
Growth Conditions ◽  
Particulate Fraction ◽  
Alcohol Dehydrogenase Activity ◽  
Ethanol Medium ◽  
Total Alcohol

Saccharomyces fragilis, a yeast capable of fermentation, grows poorly on ethanol as the carbon source. The respiratory quotient for glucose of aerobically grown cultures approaches 1 and glucose does not repress the formation of mitochondria. The effect of ethanol on the oxygen consumption and the NAD (nicotinamide adenine dinucleotide)-dependent alcohol dehydrogenase activity of this yeast has been studied. The electrophoretic pattern of alcohol dehydrogenase activity on polyacrylamide gels is complex. Six bands of activity can be identified in homogenates from cultures grown on glucose. Three of these appear associated with the particulate fraction. Differences in the relative amounts of the three particulate bands of activity under different growth conditions indicate that the particulate fraction may contain more than one isozyme. The particulate fraction also exhibits alcohol oxidase activity. While ethanol and acetate stimulate the oxygen consumption of the glucose-grown cultures, the Qo2 for these substrates is much less than that for glucose. If the glucose-grown cultures are transferred to fresh ethanol medium, the Qo2 for ethanol and acetate increases to values higher than that seen for glucose. This increase does not depend on an increase in the terminal respiratory capacity of the cells. On transfer to ethanol medium there is also a marked increase in the total alcohol dehydrogenase activity, and on electrophoresis a new band of activity appears. Acetate cannot replace ethanol in producing these effects. S. fragilis also produces an NAD-dependent alcohol dehydrogenase which reacts with cinnamyl alcohol as substrate but not with ethanol.

ALCOHOL DEHYDROGENASE ACTIVITY IN ISOLATED VACUOLES OF RED BEET ROOT CELLS

Tsitologiya ◽  
2018 ◽  
Vol 60 (6) ◽  
pp. 469-475
Author(s):  
O. D. Nimaeva ◽  
◽  
E. V. Pradedova ◽  
A. B. Karpova ◽  
R. K. Salyaev ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Root Cells ◽  
Beet Root ◽  
Red Beet ◽  
Alcohol Dehydrogenase Activity
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