The purification and biochemical properties of alcohol dehydrogenase??Fast (chateau douglas)? from Drosophila melanogaster

1984 ◽  
Vol 22 (5-6) ◽  
pp. 529-549 ◽  
Author(s):  
G. K. Chambers
Keyword(s):  
Drosophila Melanogaster ◽  
Alcohol Dehydrogenase ◽  
Biochemical Properties

scholarly journals Drosophila melanogaster alcohol dehydrogenase. Biochemical properties of the NAD+-plus-acetone-induced isoenzyme conversion

1988 ◽  
Vol 251 (1) ◽  
pp. 223-227 ◽  
Author(s):  
J O Winberg ◽  
J S McKinley-McKee
Keyword(s):  
Drosophila Melanogaster ◽  
Alcohol Dehydrogenase ◽  
Fluorescence Spectra ◽  
Irreversible Process ◽  
Biochemical Properties ◽  
Conversion Process ◽  
Absorption And Fluorescence Spectra ◽  
Kinetic Methods ◽  
Covalently Linked ◽  
Rate Limiting

The NAD+ + acetone-induced isoenzyme conversion of the Drosophila melanogaster AdhS alleloenzyme was studied. Absorption and fluorescence spectra as well as electrophoretic and kinetic methods show that the conversion process proceeds through three steps. Initially a binary enzyme-NAD+ complex is formed, followed by a ternary enzyme-NAD+-acetone complex with a KEO, Ac of 1.7 M. The last step is a rate-limiting irreversible process in which NAD+ and acetone are covalently linked to the enzyme. A Vm of 2.4 min-1 was obtained at pH 8.6.

CHANGES IN LEVELS OF ALCOHOL DEHYDROGENASE DURING THE DEVELOPMENT OF DROSOPHILA MELANOGASTER

1981 ◽  
Vol 23 (2) ◽  
pp. 305-313 ◽  
Author(s):  
Steven M. Anderson ◽  
John F. McDonald
Keyword(s):  
Drosophila Melanogaster ◽  
Alcohol Dehydrogenase ◽  
Specific Activity ◽  
Biochemical Properties ◽  
Developmental Changes ◽  
Post Translational Modification ◽  
Biochemical Basis ◽  
Quantitative Changes ◽  
Adh Activity ◽  
Qualitative Changes

The results of an analysis of the biochemical basis of changes in alcohol dehydrogenase (E.C.1.1.1.1) activity over Drosophila development are presented. The data indicate that (1) the characteristic changes that occur in ADH activity over development are predominantly, if not exclusively, the result of quantitative changes in the amount of enzyme present rather than qualitative changes affecting the enzyme's specific activity and (2) the fluctuations in amount of ADH which occur during development are not the result of the only known form of post-translational modification capable of affecting the biochemical properties of the enzyme. We conclude that developmental changes in amount of ADH are most likely the result of fluctuations in the turnover of the ADH protein.

scholarly journals An Electrophoretically Cryptic Alcohol Dehydrogenase Variant in Drosophila melanogaster. III. Biochemical Properties and Comparison with Common Enzyme Forms

1981 ◽  
Vol 34 (6) ◽  
pp. 625 ◽  
Author(s):  
GK Chambers ◽  
AV Wilks ◽  
JB Gibson
Keyword(s):  
Drosophila Melanogaster ◽  
Alcohol Dehydrogenase ◽  
Substrate Specificity ◽  
Biochemical Properties ◽  
Secondary Alcohols ◽  
Heat Stable ◽  
Michaelis Constants ◽  
High Concentrations

The biochemical properties of the heat-stable alcohol dehydrogenase variant ADH-FCh.D. have been investigated and compared with those of the two common enzyme forms ADH-F and ADH-S. The results show that ADH-F and ADH-S differ with respect to substrate specificity, their response to high concentrations of secondary alcohols and their apparent Michaelis constants for three alcohols in two different buffer systems. In all these tests the enzyme ADH-FCh.D. resembles ADH-S much more closely than ADH-F.

scholarly journals The Alcohol Dehydrogenase Gene Is Nested in the outspread Locus of Drosophila melanogaster

Genetics ◽  
1996 ◽  
Vol 143 (2) ◽  
pp. 897-911 ◽  
Author(s):  
S McNabb ◽  
S Greig ◽  
T Davis
Keyword(s):  
Drosophila Melanogaster ◽  
Alcohol Dehydrogenase ◽  
Pcr Amplification ◽  
Transcription Unit ◽  
Adjacent Gene ◽  
Dehydrogenase Gene ◽  
Chromosomal Breakpoints ◽  
Splicing Patterns ◽  
Somatic Musculature

Abstract This report describes the structure and expression of the outspread (osp) gene of Drosophila melanogaster. Previous work showed that chromosomal breakpoints associated with mutations of the osp locus map to both sides of the alcohol dehydrogenase gene (Adh), suggesting that Adh and the adjacent gene Adh' are nested in osp. We extended a chromosomal walk and mapped additional osp mutations to define the maximum molecular limit of osp as 119 kb. We identified a 6-kb transcript that hybridizes to osp region DNA and is altered or absent in osp mutants. Accumulation of this RNA peaks during embryonic and pupal periods. The osp cDNAs comprise two distinct classes based on alternative splicing patterns. The 5′ end of the longest cDNA was extended by PCR amplification. When hybridized to the osp walk, the 5′ extension verifies that Adh and Adh' are nested in osp and shows that osp has a transcription unit of ≥74 kb. In situ hybridization shows that osp is expressed both maternally and zygotically. In the ovary, osp is transcribed in nurse cells and localized in the oocyte. In embryos, expression is most abundant in the developing visceral and somatic musculature.

scholarly journals GENETIC AND BIOCHEMICAL BASIS OF ENZYME ACTIVITY VARIATION IN NATURAL POPULATIONS. I. ALCOHOL DEHYDROGENASE IN DROSOPHILA MELANOGASTER

Genetics ◽  
1978 ◽  
Vol 89 (2) ◽  
pp. 371-388
Author(s):  
John F McDonald ◽  
Francisco J Ayala
Keyword(s):  
Gene Regulation ◽  
Drosophila Melanogaster ◽  
Alcohol Dehydrogenase ◽  
Natural Populations ◽  
Difficult Problem ◽  
Regulatory Genes ◽  
Biochemical Basis ◽  
Evolutionary Consequence ◽  
The Third ◽  
Adh Activity

ABSTRACT Recent studies by various authors suggest that variation in gene regulation may be common in nature, and might be of great evolutionary consequence; but the ascertainment of variation in gene regulation has proven to be a difficult problem. In this study, we explore this problem by measuring alcohol dehydrogenase (ADH) activity in Drosophila melanogaster strains homozygous for various combinations of given second and third chromosomes sampled from a natural population. The structural locus (Adh) coding for ADH is on the second chromosome. The results show that: (1) there are genes, other than Adh, that affect the levels of ADH activity; (2) at least some of these "regulatory" genes are located on the third chromosome, and thus are not adjacent to the Adh locus; (3) variation exists in natural populations for such regulatory genes; (4) the effect of these regulatory genes varies as they interact with different second chromosomes; (5) third chromosomes with high-activity genes are either partially or completely dominant over chromosomes with low-activity genes; (6) the effects of the regulatory genes are pervasive throughout development; and (7) the third chromosome genes regulate the levels of ADH activity by affecting the number of ADH molecules in the flies. The results are consistent with the view that the evolution of regulatory genes may play an important role in adaptation.

Environmental factors affecting the quantity of alcohol dehydrogenase in Drosophila melanogaster

Nature ◽  
1979 ◽  
Vol 280 (5722) ◽  
pp. 517-518 ◽  
Author(s):  
BRYAN CLARKE ◽  
ROBERT G. CAMFIELD ◽  
ALISON M. GALVIN ◽  
CHRISTOPHER R. PITTS
Keyword(s):  
Drosophila Melanogaster ◽  
Environmental Factors ◽  
Alcohol Dehydrogenase ◽  
Factors Affecting

Properties of genetically polymorphic isozymes of alcohol dehydrogenase in Drosophila melanogaster

1974 ◽  
Vol 11 (2) ◽  
pp. 141-153 ◽  
Author(s):  
Thomas H. Day ◽  
P. C. Hillier ◽  
Bryan Clarke
Keyword(s):  
Drosophila Melanogaster ◽  
Alcohol Dehydrogenase

scholarly journals Selection for Ethanol Tolerance in Two Populations of Drosophila Melanogaster Segregating Alcohol Dehydrogenase Allozymes

1979 ◽  
Vol 32 (3) ◽  
pp. 387 ◽  
Author(s):  
John B Gibson ◽  
NigeI Lewis ◽  
MichaeI Adena ◽  
Susan R Wilson
Keyword(s):  
Drosophila Melanogaster ◽  
Alcohol Dehydrogenase ◽  
Ethanol Tolerance ◽  
Selection For ◽  
Two Populations

Selection for ethanol tolerance was equally successful in two populations of D. melanogaster in both of which the frequency of AdhF was 0�5 at the start of the experiment.

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