scholarly journals Allyl Alcohol Selection for Lower Alcohol Dehydrogenase Activity in Nicotiana plumbaginifolia Cultured Cells

1988 ◽  
Vol 86 (1) ◽  
pp. 266-269 ◽  
Author(s):  
Jack M. Widholm ◽  
Isao Kishinami
Keyword(s):  
Alcohol Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Allyl Alcohol ◽  
Cultured Cells ◽  
Nicotiana Plumbaginifolia ◽  
Lower Alcohol ◽  
Alcohol Dehydrogenase Activity ◽  
Allyl Alcohol Selection ◽  
Selection For

scholarly journals Inducible UDP-glucose dehydrogenase from French bean (Phaseolus vulgaris L.) locates to vascular tissue and has alcohol dehydrogenase activity

1996 ◽  
Vol 313 (1) ◽  
pp. 311-317 ◽  
Author(s):  
Duncan ROBERTSON ◽  
Colin SMITH ◽  
G. Paul BOLWELL
Keyword(s):  
Alcohol Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Vascular Tissue ◽  
Cultured Cells ◽  
Peptide Mapping ◽  
Glucose Dehydrogenase ◽  
Gel Filtration ◽  
French Bean ◽  
Suspension Cultured Cells ◽  
Alcohol Dehydrogenase Activity

UDP-glucose dehydrogenase is responsible for channelling UDP-glucose into the pool of UDP-sugars utilized in the synthesis of wall matrix polysaccharides and glycoproteins. It has been purified to homogeneity from suspension-cultured cells of French bean by a combination of hydrophobic-interaction chromatography, gel filtration and dye-ligand chromatography. The enzyme had a subunit of Mr 40000. Km values were measured for UDP-glucose as 5.5±1.4 mM and for NAD+ as 20±3 μM. It was subject to inhibition by UDP-xylose. UDP-glucose dehydrogenase activity co-purified with alcohol dehydrogenase activity from suspension-cultured cells, elicitor-treated cells and elongating hypocotyls, even when many additional chromatographic steps were employed subsequently. The protein from each source was resolved into virtually identical patterns of isoforms on two-dimensional isoelectric focusing/PAGE. However, a combination of peptide mapping and sequence analysis, gel analysis using activity staining and kinetic analysis suggests that both activities are a function of the same protein. An antibody was raised and used to immunolocalize UDP-glucose dehydrogenase to developing xylem and phloem of French bean hypocotyl. Together with data published previously, these results are consistent with an important role in the regulation of carbon flux into wall matrix polysaccharides.

scholarly journals Alcohol dehydrogenase activity in Drosophila melanogaster: a quantitative character

1975 ◽  
Vol 26 (1) ◽  
pp. 81-93 ◽  
Author(s):  
R. D. Ward
Keyword(s):  
Drosophila Melanogaster ◽  
Alcohol Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Structural Gene ◽  
Genetic Background ◽  
Quantitative Character ◽  
Alcohol Dehydrogenase Activity ◽  
Activity Modifiers ◽  
Selection For ◽  
Adh Activity

SUMMARYAlcohol dehydrogenase activity in Drosophila melanogaster may be considered as a quantitative character, since it shows many features typically associated with such traits. Although strains with the electrophoretically fast phenotype generally have activities greater than those with the slow phenotype, presumably reflecting differences in the nucleotide sequences of the structural alleles, within each electrophoretic class there is considerable variation in activity. The expression of the structural gene, in terms of ADH activity, is to some extent regulated by its genetic background. Strains homozygous for particular structural alleles respond to divergent directional selection for ADH activity. Modifiers have been located to the X, second and third chromosomes.

Escherichia coli mutants with a temperature-sensitive alcohol dehydrogenase

1982 ◽  
Vol 152 (2) ◽  
pp. 935-938
Author(s):  
W Lorowitz ◽  
D Clark
Keyword(s):  
Escherichia Coli ◽  
Alcohol Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Allyl Alcohol ◽  
Temperature Sensitive ◽  
Acetaldehyde Dehydrogenase ◽  
Regulatory Locus ◽  
Alcohol Dehydrogenase Activity

Mutants of Escherichia coli resistant to allyl alcohol were selected. Such mutants were found to lack alcohol dehydrogenase. In addition, mutants with temperature-sensitive alcohol dehydrogenase activity were obtained. These mutations, designated adhE, are all located at the previously described adh regulatory locus. Most adhE mutants were also defective in acetaldehyde dehydrogenase activity.

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

Elevation of Alcohol Dehydrogenase Activity in the Subclinically Scorbutic Guinea-Pig

1972 ◽  
Vol 42 (6) ◽  
pp. 781-784 ◽  
Author(s):  
Maureen O'keane ◽  
M. R. Moore ◽  
A. Goldberg
Keyword(s):  
Alcohol Dehydrogenase ◽  
Guinea Pig ◽  
Dehydrogenase Activity ◽  
Guinea Pigs ◽  
Liver Protein ◽  
Alcohol Dehydrogenase Activity ◽  
Nadh Ratio

1. Because it has been shown that a majority of alcoholics are subclinically scorbutic, the metabolism of ethanol was studied in subclinically-scorbutic guinea-pigs. 2. Hepatic alcohol dehydrogenase activity was raised maximally by ethanol within 2 days. 3. In twenty-three subclinically-scorbutic guinea-pigs fed ethanol for 2 weeks, the alcohol dehydrogenase activity (±SD) was 11·5 ± 1·2 units/g of liver protein compared with 8·6 ± 0·6 units/g of liver protein in twenty-three healthy animals fed ethanol. 4. The NAD+/NADH ratio in subclinically-scorbutic guinea-pigs and healthy guinea-pigs fed ethanol, shows that there is more NAD+ available for oxidation of alcohol in subclinically-scorbutic guinea-pigs. These results may explain the increased tolerance of alcoholics to alcohol.

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