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  • 1
    Electronic Resource
    Electronic Resource
    Bradford : Emerald
    Engineering computations 17 (2000), S. 459-486 
    ISSN: 0264-4401
    Source: Emerald Fulltext Archive Database 1994-2005
    Topics: Technology
    Notes: The production of steel pipes with guaranteed external collapse pressure (e.g. high collapse casings for oil wells) requires the implementation of an accurate process control. To develop that process control it is necessary to investigate how different parameters affect the external collapse pressure of the pipes. Experimental/numerical techniques implemented to investigate the collapse behavior of steel pipes are presented. The discussion of the experimental techniques includes the description of the facilities for performing external pressure collapse tests and the description of an imperfections measuring system. The numerical techniques include 2D and 3D finite element models. The effects on the value of the pipes' external collapse pressure of their shape, residual stresses and material properties are discussed.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1617-4623
    Keywords: APRT ; Drosophila ; Nuclear matrix attachment site ; Dosage compensation ; Introns
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The Aprt locus of Drosophila encodes the structural gene for the purine salvage enzyme adenine phosphoribosyltransferase. Aprt is autosomal and enzyme activity is gene-dose-dependent in Drosophila melanogaster. However, Aprt is X-linked and dosage compensated in Drosophila pseudoobscura, as shown here. The Aprt genes of both Drosophila species contain a DNA sequence associated with nuclear matrix attachment sites and these Aprt sequences specifically bind to nuclear matrix in vitro. Putative promoter sequences positioned upstream of the predicted transcriptional start site in the two Aprt genes have a similar structure of direct repeats with an overlapping dyad symmetry, but the DNA sequence of these motifs is not conserved between the two species. Biological features in mutants of Aprt as well as natural variants suggest that dosage compensation of this gene in Drosophila pseudoobscura is due to a general control Mechanism on X-linked genes rather than a gene-specific mechanism.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0192-253X
    Keywords: urate oxidase ; 20-hydroxyecdysone ; Drosophila melanogaster ; Malpighian tubules ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The tissue-specific enzyme urate oxidase is confined exclusively to the Malpighian tubules of Drosophila melanogaster and expressed only in the third-instar larva and the adult. Shortly before pupariation urate oxidase activity declines precipitously and is not detectable 24 hours later. That 20-hydroxyecdysone is the factor that triggers the disappearance of urate oxidase activity in late third-instar larvae is demonstrated using the temperature sensitive mutant ecd1 which at the nonpermissive temperature of 29°C fails to accumulate a sufficient concentration of 20-hydroxyecdysone necessary for puparium formation and thus remains a third-instar larva for 1 to 2 weeks before death. Both the life cycle and the temporal profile of urate oxidase activity in ecd1 larvae at 19°C is identical to that of the wild type. However, at 29°C ecd1 third-instar larvae retain high urate oxidase activity. A precipitous decline in urate oxidase activity is observed when ecd1 larvae at 29°C are fed 20-hydroxyecdysone. These data implicate 20-hydroxyecdysone in the process that controls the rapid decline of urate oxidase activity at the time of puparium formation. In whole homogenates of Malpighian tubules, the urate oxidase polypeptide was identified in SDS-polyacrylamide gels by its Rf with respect to homogeneously pure Drosophila urate oxidase and also by immunoprecipitation with rabbit anti-Drosophila urate oxidase IgG. Throughout development the amount of the urate oxidase polypeptide is correlated with the magnitude of urate oxidase activity.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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