Oviposition-site preference and ADH activity in Drosophila melanogaster View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1982-03

AUTHORS

N. Hougouto, M. C. Liétaert, M. Libion-Mannaert, E. Feytmans, A. Elens

ABSTRACT

Four D. melanogaster strains characterized by different alcohol dehydrogenase (ADH) activities were compared for their oviposition site preferences. The comparison was made between different temperatures (15 °C, 20 °C, 25 °C, 30 °C), day and night, replicates, and different concentrations in ethanol (00%, 5%, 10%, 15%) in the medium. All these factors influence behaviour. ADH activities seem to affect the oviposition site preferences as they directly affect ethanol tolerance and the ability to use alcohol as a source of metabolic energy. More... »

PAGES

121-128

References to SciGraph publications

  • 1973-12. Genetical variation for enzyme activity in a population of Drosophila melanogaster in HEREDITY
  • 1979-05. Oviposition site preference inDrosophila in BEHAVIOR GENETICS
  • 1970-08. Enzyme Flexibility in Drosophila melanogaster in NATURE
  • 1980-05. Relationship between ADH activity and behavioral response to environmental alcohol inDrosophila in BEHAVIOR GENETICS
  • 1976-01. Ethanol as a ‘food’ forDrosophila melanogaster: Influence of theEbony gene in CELLULAR AND MOLECULAR LIFE SCIENCES
  • 1974-02. The relative quantities and catalytic activities of enzymes produced by alleles at the alcohol dehydrogenase locus in Drosophila melanogaster in BIOCHEMICAL GENETICS
  • 1978-04. Alcohol metabolism in Drosophila melanogaster: Uselessness of the most active aldehyde oxidase produced by the Aldox locus in BIOCHEMICAL GENETICS
  • 1975. Gene-Enzyme Systems in Drosophila in NONE
  • 1980-01. Behavior genetics of choice of oviposition sites inDrosophila melanogaster. I. Genetic variability and analysis of behavior in BEHAVIOR GENETICS
  • 1976-12. Biological role of alcohol dehydrogenase in the tolerance of Drosophila melanogaster to aliphatic alcohols: Utilization of an ADH-null mutant in BIOCHEMICAL GENETICS
  • 1975-10. Similarities and differences in latitudinal adaptation of two Drosophila sibling species in NATURE
  • 1973-07. Isozyme variability in species of the genus Drosophila. VI. Frequency-property-environment relationships of allelic alcohol dehydrogenases in D. melanogaster in BIOCHEMICAL GENETICS
  • 1976-04. Evidence for the adaptive significance of enzyme activity levels: Interspecific variation in α-GPDH and ADH in Drosophila in BIOCHEMICAL GENETICS
  • 1979-05. Ethanol metabolism inDrosophila melanogaster in CELLULAR AND MOLECULAR LIFE SCIENCES
  • 1978-06. Alcohol dehydrogenase polymorphism in populations of Drosophila melanogaster. II. Relation between ADH activity and adult mortality in BIOCHEMICAL GENETICS
  • 1972-04. Variability of Alcohol Dehydrogenase Activity in a Natural Population of Drosophila melanogaster in NATURE
  • 1972-12. Alcohol tolerance: An ecological parameter in the relative success of Drosophila melanogaster and Drosophila simulans in OECOLOGIA
  • Journal

    TITLE

    Genetica

    ISSUE

    2

    VOLUME

    58

    Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/bf00056779

    DOI

    http://dx.doi.org/10.1007/bf00056779

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1015695172


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