Variation in alcohol dehydrogenase activity in vitro in flies from natural populations ofDrosophila melanogaster

Genetica ◽  
1985 ◽  
Vol 67 (1) ◽  
pp. 13-19 ◽  
Author(s):  
D. G. Anderson ◽  
J. B. Gibson
1976 ◽  
Vol 29 (4) ◽  
pp. 389 ◽  
Author(s):  
ADH Brown ◽  
DR Marshall ◽  
J Munday

Alcohol dehydrogenase is highly polymorphic in many plant and animal species. Here we report evidence that the naturally occurring, electrophoretically detectable allozyme variants of the AdhlB locus in B. mollis can respond differentially to environmental stresses. It is argued that alcohol dehydrogenase activity is specifically involved in response to these stresses. Crude extracts of predominantly selfed seeds sampled from plants of known Adh1B genotype were assayed for their ADH activity in the forward and backward reactions. The seeds from Adh~B Adh~B plants produced extracts about 12 % less active in both directions than seeds from their Adh~BAdh~B counterparts. Such Adh~BAdh~B plants were also shown to produce about 13% more dry matter when grown under continuous flooding in the greenhouse whereas no difference between genotypes was detected in control pots. The seeds of Adh~B Adh~B plants showed an advantage over the alternative homozygotes in more rapid germination at 2�C, but no difference was found at 15�C. Thus the variants are differentially adapted, and this is likely to playa role in the maintenance of the polymorphism in natural populations.


1976 ◽  
Vol 54 (6) ◽  
pp. 539-545 ◽  
Author(s):  
G. W. Forsyth ◽  
H. T. Nagasawa ◽  
C. S. Alexander

Rat hearts perfused with oxygenated buffer containing [1-14C]ethanol metabolized small amounts of the ethanol to carbon dioxide. Very sensitive techniques are required to separate the resulting 14CO2 from the ethanol. This metabolism is not inhibited by levels of pyrazole which markedly inhibit NAD dependent liver alcohol dehydrogenase (EC 1.1.1.1). In vitro studies suggest that NADP functions as a cofactor for the rat heart alcohol dehydrogenase activity of crude heart homogenates. The kinetic parameters, the specific activity, and the pH dependence of the enzyme activity measured in these experiments suggest that it may have a minor role in ethanol metabolism by the rat.


1979 ◽  
Vol 17 (5-6) ◽  
pp. 553-563 ◽  
Author(s):  
Ira Papel ◽  
Melford Henderson ◽  
Jeanine Van Herrewege ◽  
Jean David ◽  
William Sofer

1980 ◽  
Vol 33 (1) ◽  
pp. 105 ◽  
Author(s):  
JG Oakeshott ◽  
JB Gibson ◽  
PR Anderson ◽  
A Champ

Three experiments have been carried out which show that exogenous environments of ethanol impose selection on the alcohol dehydrogenase (Adh) locus of D. melanogaster. This locus is widely polymorphic for two alleles, AdhF and Adhs, and AdhF generally produces about twice as much alcohol dehydrogenase activity as Adhs. In the first experiment, AdhF IAdhF and AdhF/Adhs flies survived equally often and Adhs/Adhs flies less frequently after exposure for 7 days to medium impregnated with ethanol. The same pattern of survival differences was found in the second experiment in which flies were exposed for 1 day to an aqueous solution of ethanol and sucrose. In contrast, in the third experiment survival was scored after exposure for 45-min to ethanol fumes, and Adhs/ Adhs flies survived more often than AdhF/Adhs, both these genotypes surviving more frequently than Adh F / Adh F. We doubt whether anyone of the three experiments by itself adequately represents the ecology of natural populations of D. melanogaster exposed to ethanol. It is likely that mixtures of the three experimental conditions approximate more closely the natural environments and therefore we suggest that, overall, selection might favour intermediate levels of alcohol dehydrogenase activity, producing a net advantage for heterozygotes at the Adh locus.


1980 ◽  
Vol 186 (2) ◽  
pp. 483-490 ◽  
Author(s):  
Gloria Rachamin ◽  
J. Alain Macdonald ◽  
Samina Wahid ◽  
Jeremy J. Clapp ◽  
Jatinder M. Khanna ◽  
...  

In young (4-week-old) male and female spontaneously hypertensive (SH) rats, ethanol metabolic rate in vivo and hepatic alcohol dehydrogenase activity in vitro are high and not different in the two sexes. In males, ethanol metabolic rate falls markedly between 4 and 10 weeks of age, which coincides with the time of development of sexual maturity in the rat. Alcohol dehydrogenase activity is also markedly diminished in the male SH rat and correlates well with the changes in ethanol metabolism. There is virtually no influence of age on ethanol metabolic rate and alcohol dehydrogenase activity in the female SH rat. Castration of male SH rats prevents the marked decrease in ethanol metabolic rate and alcohol dehydrogenase activity, whereas ovariectomy has no effect on these parameters in female SH rats. Chronic administration of testosterone to castrated male SH rats and to female SH rats decreases ethanol metabolic rate and alcohol dehydrogenase activity to values similar to those found in mature males. Chronic administration of oestradiol-17β to male SH rats results in marked stimulation of ethanol metabolic rate and alcohol dehydrogenase activity to values similar to those found in female SH rats. Chronic administration of ethanol to male SH rats from 4 to 11 weeks of age prevents the marked age-dependent decreases in ethanol metabolic rate and alcohol dehydrogenase activity, but has virtually no effect in castrated rats. In the intoxicated chronically ethanol-fed male SH rats, serum testosterone concentrations are significantly depressed. In vitro, testosterone has no effect on hepatic alcohol dehydrogenase activity of young male and female SH rats. In conclusion, in the male SH rat, ethanol metabolic rate appears to be limited by alcohol dehydrogenase activity and is modulated by testosterone. Testosterone has an inhibitory effect and oestradiol has a testosterone-dependent stimulatory effect on alcohol dehydrogenase activity and ethanol metabolic rate in these animals.


Tsitologiya ◽  
2018 ◽  
Vol 60 (6) ◽  
pp. 469-475
Author(s):  
O. D. Nimaeva ◽  
◽  
E. V. Pradedova ◽  
A. B. Karpova ◽  
R. K. Salyaev ◽  
...  

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