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  • Drosophila  (2)
  • Springer  (2)
  • American Association for the Advancement of Science
  • Oxford University Press
  • Wiley-Blackwell
  • 1985-1989  (1)
  • 1975-1979  (1)
  • 1950-1954
Collection
Publisher
  • Springer  (2)
  • American Association for the Advancement of Science
  • Oxford University Press
  • Wiley-Blackwell
Years
  • 1985-1989  (1)
  • 1975-1979  (1)
  • 1950-1954
Year
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 13 (1975), S. 353-356 
    ISSN: 1573-4927
    Keywords: suppression ; Drosophila ; phenol oxidase ; speck
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A marked decrease in the amount of the A2 component of phenol oxidase occurs in the speck locus of Drosophila melanogaster. The amount of A2 in speck is restored to a normal amount in the presence of the suppressor mutant, su(s) 2.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 213 (1988), S. 505-512 
    ISSN: 1617-4623
    Keywords: Drosophila ; Molybdoenzymes ; cinnamon
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mutations at the cin gene display drastically lowered levels of the molybdoenzymes, xanthine dehydrogenase (XDH) and aldehyde oxidase (AO), and lack pyridoxal oxidase (PO) and sulfite oxidase (SO) activities. Certain mutations at cin also display varying degrees of female sterility, which is maternally affected. Here we characterize five new cin alleles with respect to the molybdoenzyme activities as well as the molybdenum cofactor, commonly required for molybdoenzyme activity. In complementing cin heterozygotes we find that, in addition to the previously reported unusually high levels of XDH and AO activities, there are unusually elevated levels of SO activity, as well as complementation for PO activity. The levels of immunologically crossreacting material in such heterozygotes indicate that the elevated levels of molybdoenzyme activities cannot be due to increases in the number of enzyme molecules. Measurements of the level of molybdenum cofactor activity normally present in XDH, AO, PO, and SO point to the possibility that a larger fraction of the enzyme molecules are active in these heterozygotes. The possible role of SO with respect to cinnamon's female sterility is also discussed.
    Type of Medium: Electronic Resource
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