Hostname: page-component-586b7cd67f-tf8b9 Total loading time: 0 Render date: 2024-11-24T08:09:46.867Z Has data issue: false hasContentIssue false
  • English
  • Français

Alcohol dehydrogenase activity in Drosophila melanogaster: a quantitative character

Published online by Cambridge University Press:  14 April 2009

R. D. Ward
R. D. Ward
Affiliation:
Department of Genetics, University of Cambridge, Cambridge CB4 1XH, U.K.
Rights & Permissions [Opens in a new window]

Summary

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

Alcohol 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.

Type
Research Article
Information
Genetics Research , Volume 26 , Issue 1 , August 1975 , pp. 81 - 93
Copyright
Copyright © Cambridge University Press 1975

References

REFERENCES

Birley, A. J. & Barnes, B. W. (1973). Genetical variation for enzyme activity in a population of Drosophila melanogaster. 1. Extent of the variation for alcohol dehydrogenase activity. Heredity 31, 413–416.CrossRefGoogle Scholar
Briscoe, D. A., Robertson, A. & Malpica, J.-M. (1975). Dominance at Adh locus in response of adult Drosophila melanogaster to environmental alcohol. Nature 255, 148–149.CrossRefGoogle ScholarPubMed
Day, T. H., Hillier, P. C. & Clarke, B. (1974). The relative quantities and catalytic activities of enzymes produced by alleles at the alcohol dehydrogenase locus in Drosophila melanogaster. Biochemical Genetics 11, 155–165.CrossRefGoogle ScholarPubMed
van Delden, W., Kamping, A. & van Dijk, H. (1975). Selection at the alcohol dehydrogenase locus in Drosophila melanogaster. Experientia 31, 418–419.CrossRefGoogle Scholar
Gibson, J. B. (1970). Enzyme flexibility in Drosophila melanogaster. Nature 227, 959–960.CrossRefGoogle ScholarPubMed
Gibson, J. B. & Miklovich, R. (1971). Modes of variation in alcohol dehydrogenase in Drosophila melanogaster. Experientia 27, 99–100.CrossRefGoogle ScholarPubMed
Grell, E. H., Jacobson, K. B. & Murphy, J. B. (1965). Alcohol dehydrogenase in Drosophila melanogaster: Isozymes and genetic variants. Science 149, 80–82.CrossRefGoogle ScholarPubMed
Hewitt, N. E., Pipkin, S. B., Williams, N. & Chakrabartty, P. K. (1974). Variation in ADH activity in Class 1 and Class 11 strains of Drosophila. The Journal of Heredity 65, 141–148.CrossRefGoogle Scholar
Johnson, F. M. & Denniston, C. (1964). Genetic variation of alcohol dehydrogenase in Drosophila melanogaster. Nature 204, 906–907.CrossRefGoogle Scholar
Keller, E. C. (1964). Quantitative differences in xanthine dehydrogenase activity in wild type strains of Drosophila melanogaster. Molecular and General Genetics 95, 326–332.CrossRefGoogle ScholarPubMed
Keller, E. C. & Mitchell, D. F. (1962). Interchromosomal genotypic interactions. 1. An analysis of morphological characters. Genetics 47, 1557–1571.CrossRefGoogle Scholar
Komma, D. J. (1966). Effect of sex transformation genes on glucose-6-phosphate dehydrogenase activity in Drosophila melanogaster. Genetics 54, 497–503.CrossRefGoogle ScholarPubMed
Lewis, H. W. & Lewis, H. S. (1963). Genetic regulation of dopaoxidase activity in Drosophila. Annals of the New York Academy of Sciences 100, part 11, 827–839.CrossRefGoogle Scholar
Lindsley, D. L. & Grell, E. H. (1968). Genetic variations of Drosophila melanogaster. Carnegie Institution of Washington. Publication 552, 1944.Google Scholar
Milkman, R. & Zeitler, R. R. (1974). Concurrent multiple paternity in natural and laboratory populations of Drosophila melanogaster. Genetics 78, 1191–1193.CrossRefGoogle Scholar
Morgan, P. (1974). Selection acting directly on an enzyme polymorphism. Heredity 34, 124–127.CrossRefGoogle Scholar
Rasmuson, B., Nilson, L. R., Rasmuson, M. & Zeppezauer, E. (1966). Effects of hetero-zygosity on alcohol dehydrogenase (ADH) activity in Drosophila. Hereditas 56, 313–316.CrossRefGoogle Scholar
Ursprung, H., Sofer, W. H. & Burroughs, N. (1970). Ontogeny and tissue distribution of alcohol dehydrogenase in Drosophila melanogaster. Wilhelm Roux Archiv' für Entwick-lungsmechanik der Organismen 164, 201–208.CrossRefGoogle Scholar
Ward, R. D. (1974). Alcohol dehydrogenase in Drosophila melanogaster: activity variation in natural populations. Biochemical Genetics 12, 449–458.CrossRefGoogle ScholarPubMed
Ward, R. D. & Hebert, P. D. N. (1972). Variability of alcohol dehydrogenase activity in a natural population of Drosophila melanogaster. Nature New Biology 236, 243–244.CrossRefGoogle Scholar