The effect of temperature on biochemical and molecular properties ofDrosophila alcohol dehydrogenase

1986 ◽  
Vol 24 (11-12) ◽  
pp. 873-889 ◽  
Author(s):  
Kevin C. McElfresh ◽  
John F. McDonald
Keyword(s):  
Alcohol Dehydrogenase ◽  
Molecular Properties ◽  
Effect Of Temperature

scholarly journals Drosophila alcohol dehydrogenase frequencies and temperature

1978 ◽  
Vol 31 (1) ◽  
pp. 97-101 ◽  
Author(s):  
Maria A. Gionfriddo ◽  
Charles L. Vigue
Keyword(s):  
Environmental Factors ◽  
Alcohol Dehydrogenase ◽  
Correlation Coefficients ◽  
Effect Of Temperature ◽  
Early Fall

SUMMARYD. melanogaster imagoes were collected weekly throughout the summer and early fall of 1976. Their Adh genotypes were determined by electrophoresis. The frequency of the Adh4 isoallele fluctuated throughout the period of study. Correlation coefficients assuming no delay, one week delay, two weeks' delay, three weeks' delay, and a four-week delay of the effect of temperature on the frequency of the Adh4 isoallele were insignificant. It was concluded that temperature alone may not be a selective factor but may be selective in combination with other environmental factors.

scholarly journals The relative conformational stability of the alcohol dehydrogenase alleloenzymes of the fruitfly Drosophila melanogaster

1981 ◽  
Vol 197 (1) ◽  
pp. 111-117 ◽  
Author(s):  
D R Thatcher ◽  
R Sheikh
Keyword(s):  
Drosophila Melanogaster ◽  
Alcohol Dehydrogenase ◽  
Conformational Stability ◽  
Effect Of Temperature ◽  
Net Charge ◽  
Subunit Dissociation ◽  
Naturally Occurring ◽  
Transverse Temperature ◽  
The Stability ◽  
Temperature Optima

The effect of temperature on four purified alleloenzymes of the alcohol dehydrogenase (Adhs, Adhf, AdhD and Adhn-5) of the fruitfly Drosophila melanogaster was investigated in detail. Initial-velocity studies showed that the naturally occurring Adhf and Adhs enzymes differed only in their temperature optima, and evidence of kinetic adaptation to high and low temperature was not apparent. All four alleloenzymes denatured irreversibly on heating purified enzyme solutions at pH 6.0. This technique revealed only small differences in thermostability between Adhf and Adhs, although the two mutant enzymes from AdhD and Adhn-5 were considerably more labile. Electrophoresis of the enzymes though a stable transverse temperature gradient proved to be a discriminating and reproducible technique. Enzymes of different net charge were compared on the same polyacrylamide gel. The Adhf enzyme was shown to be significantly less stable than the Adhs enzyme. Subunit interchange was observed at temperatures below the point at which the unfolding occurred. At pH 4.0, the Adhf/Adhs heterodimer was as stable as the Adhs homodimeric enzyme, and more stable than the Adhf homodimer. Adhn-5 and AdhD alleloenzymes were relatively thermolabile. The stability of the alleloenzymes towards urea denaturation was studied by urea-gradient electrophoresis. Only small differences in stability between the Adhf and Adhs enzymes were observed. The AdhD and Adhn-5 mutants were denatured at the same urea concentration, which was much lower than in the case of the wild-type enzymes. Except at pH 4.0, subunit dissociation could not be distinguished from the unfolding of the monomer.

Human liver .pi.-Alcohol dehydrogenase: kinetic and molecular properties

Biochemistry ◽  
1979 ◽  
Vol 18 (6) ◽  
pp. 1101-1105 ◽  
Author(s):  
William F. Bosron ◽  
Ting-Kai Li ◽  
Werner P. Dafeldecker ◽  
Bert L. Vallee
Keyword(s):  
Alcohol Dehydrogenase ◽  
Human Liver ◽  
Molecular Properties

scholarly journals BIOCHEMICAL DIFFERENCES BETWEEN PRODUCTS OF THE Adh LOCUS IN DROSOPHILA

Genetics ◽  
1980 ◽  
Vol 95 (4) ◽  
pp. 1013-1022
Author(s):  
John F McDonald ◽  
Steven M Anderson ◽  
Mauro Santos
Keyword(s):  
Alcohol Dehydrogenase ◽  
Natural Populations ◽  
Adaptive Significance ◽  
Molecular Properties

ABSTRACT An analysis of the molecular properties of the major alcohol dehydrogenase (E.C.1.1.1.1) allozyme variants found segregating in natural populations of D. melanogaster is presented. Our results indicate: (1) ADH-S enzyme has generally lower Michaelis-Menten constants than those of ADH-F; (2) ADH-S and ADH-F enzymes display opposite interactions for both co-factor and substrate; and (3) higher levels of ADH are associated with the Adh-fast genotype. The possible adaptive significance of these findings is discussed.

Effect of pH and temperature on alcohol dehydrogenase

1979 ◽  
Vol 44 (3) ◽  
pp. 986-990 ◽  
Author(s):  
Sylva Leblová ◽  
Roman Lapka ◽  
Noemi Nováková
Keyword(s):  
Alcohol Dehydrogenase ◽  
Reaction Rate ◽  
Ethanol Oxidation ◽  
Effect Of Temperature ◽  
Effect Of Ph ◽  
Michaelis Constants ◽  
Pea Seeds ◽  
Increasing Temperature

Alcohol dehydrogenase isolated from germinating pea seeds catalyzes ethanol oxidation at pH 8.7 and acetaldehyde reduction at pH 7.0. The values of the Michaelis constants are the lowest in the range of pH-optimums. The effect of temperature on the reaction rate was investigated over the range 15-55 °C. The initial and maximal rates increase with the increasing temperature and attain a maximum at 40 °C. The values of the Michaelis constants are the lowest at 21 °C. Pea alcohol dehydrogenase looses its activity at 70 °C, the binary enzyme-NAD complex is more thermostable.

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