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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Development genes and evolution 190 (1981), S. 118-122 
    ISSN: 1432-041X
    Keywords: Drosophila ; Aggregation ; Lectins ; Cell surface ; Embryo-derived cell line
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In this paper we describe the aggregation of cells from embryo-derived cell lines ofDrosophila, measured by examining the ability of single cells to adhere to one another when suspended in culture medium and swirled on a rotary shaker. Using this method we demonstrated the presence of receptors for Concanavalin A, soybean agglutinin, and possibly wheat germ agglutinin on the surface of Schneider's line-2 cells. Our work provides basic descriptive and background information for further studies onDrosophila cells, including those isolated from imaginal discs.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-4927
    Keywords: Drosophila ; rudimentary ; aspartate transcarbamylase ; dihydroorotase ; multienzyme complex
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The activities of the enzymes aspartate transcarbamylase (ATCase) and dihydroorotase (DHOase) were determined in adult females from a wild-type strain and from eight different alleles of the X-linked mutation rudimentary (r) of Drosophila melanogaster. The alleles chosen span the genetic map of the r locus. The characteristics of the DHOase-catalyzed reaction which converts carbamyl aspartate to dihydroorotate are briefly described. Of all of the r strains tested, only one, r 9, has wild-type levels of aspartate transcarbamylase and dihydroorotase activities. The other seven show either intermediate or very low levels of activity for both enzymes. The lowered ATCase and DHOase activities observed in mutants which do not map in the region of the structural gene for these enzymes are interpreted in light of recent evidence that ATCase and DHOase are part of a three-enzyme complex.
    Type of Medium: Electronic Resource
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