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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 19 (1981), S. 567-583 
    ISSN: 1573-4927
    Keywords: aldehyde oxidase ; Drosophila ; evolution ; gene regulation ; isozymes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract At least four enzymes contribute to histochemically, electrophoretically, or spectrophotometrically detectable aldehyde oxidase (AO) activity in Drosophila melanogaster. The one we designate AO-1 contributes the majority of activity measured in extracts of whole flies. Pyridoxal oxidase (PO) is also a broad range AO. It is prominent only in midgut and Malpighian tubules, where it apparently accounts for a substantial fraction of total AO activity. The tissue distributions of these enzymes are clearly disparate despite close linkage of their structural loci and parallel dependence on the mal, lxd, and cin loci. A similarly related enzyme, xanthine dehydrogenase (XDH), is detected as an AO only in electrophoretic gels. A fourth broad range AO, not dependent on mal, lxd, and cin, is confined to the ejaculatory bulb. A similar array of AO isozymes is present in phylogenetically distant Drosophila species.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 1 (1979), S. 229-240 
    ISSN: 0192-253X
    Keywords: aldehyde oxidase ; alcohol dehydrogenase ; Hawaiian Drosophila ; interspecific hybridization ; regulatory genes ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Drosophila heteroneura and D differens are closely related, interfertile species of the Hawaiian picture-winged group. They display marked qualitative and quantitative differences in the pattern of expression of alcohol dehydrogenase (ADH) and an aldehyde oxidase (AO-1). These presumptive regulatory differences are revealed by comparisons of the relative levels of these enzymes in various tissues in larvae and adults. In hybrids produced between parents carrying different electrophoretic alleles at the structural loci for these two enzymes, each allele is expressed according to the developmental program characteristic of the parent from which it was derived. This result indicates control of the differences in pattern of expression by one or more cis-acting sites associated with each structural locus. The distribution of activity among all the three forms of these dimeric enzymes produced in hybrids indicates that the pattern differences reflect differential accumulation of enzyme molecules, not altered catalytic properties. As expected, the regulatory differences segregate with the electrophoretic markers in backcrosses.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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