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  • Communities  (1)
  • Drosophila mojavensis  (1)
  • 1
    ISSN: 1432-1939
    Keywords: Yeast ; Drosophila ; Host plants ; Communities ; Vectors
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The yeast communities from slime fluxes of three deciduous trees (Prosopis juliflora, Populus fremontii and Quercus emoryi) and the necroses of two cacti (Opuntia phaeacantha and Carnegiea gigantea) were surveyed in the region of Tucson, Arizona. In addition, the yeasts carried by dipterans associated with the fluxes or necroses (Drosophila carbonaria, D. brooksae, D. nigrospiracula, D. mettleri, and Aulacigaster leucopeza) were sampled. The results indicate that each host sampled had a distinct community of yeasts associated with it. The dipterans, which can act as vectors of the yeasts, deposited yeasts from other sources in addition to those found on their associated hosts. It is argued that host plant physiology is relatively more important than the activity of the vector in determining yeast community composition. Furthermore, the average number of yeast species per flux or necrosis is not different from the average number of yeast species per fly. It is hypothesized that the vector may affect the number of species per individual flux or not, and that the number is lower than the rot or necrosis could potentially support.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-4927
    Keywords: Drosophila mojavensis ; alcohol dehydrogenase ; gene duplication ; isozymes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The electrophoretic pattern of alcohol dehydrogenase (ADH) of Drosophilia mojavensis is composed of multiple bands. In previous studies from this laboratory we suggested on the basis of genetic evidence that multiple ADH bands were due to the presence of a gene duplication. In the studies presented here, this hypothesis is supported by data derived from comparing the protein biochemistry of each ADH. Three forms of D. mojavensis ADH have been isolated. These are the ADH-1 homodimer, the ADH-2 homodimer, and the ADH-1 ADH-2 interlocus heterodimer. Each of these isozymes has a native molecular weight of approximately 50,000. Each native molecule is composed of two subunits of identical size, 24,000 daltons. The native molecules differ slightly in their isoelectric points. Thermal denaturation also reveals that ADH-1 and ADH-2 are slightly different, ADH-1 being somewhat more thermostable. The interlocus heterodimer has properties intermediate between those of ADH-1 and those of ADH-2. Kinetic comparison also indicates a similarity among the three isozymes. ADH-2 is somewhat better at oxidizing ethanol relative to 2-propanol as compared to ADH-1. All of our studies support the general conclusion that the isozymes of ADH found in D. mojavensis are similar to one another and to other ADH from other species of Drosophila. This supports our hypothesis that multiple bands of ADH in D. mojavensis reflect the presence of a duplication of the Adh locus in that species.
    Type of Medium: Electronic Resource
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