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  • Drosophila melanogaster  (2)
  • Computational Chemistry and Molecular Modeling
  • glycogen phosphorylase
  • Springer  (3)
  • Blackwell Publishing Ltd
  • Wiley-Blackwell
  • 1990-1994  (3)
Collection
Keywords
Publisher
  • Springer  (3)
  • Blackwell Publishing Ltd
  • Wiley-Blackwell
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    The urate oxidase gene of Drosophila pseudoobscura and Drosophila melanogaster: Evolutionary changes of sequence and regulation (1992)
    Springer
    Journal of molecular evolution 34 (1992), S. 62-77 
    Details
    ISSN: 1432-1432
    Keywords: Urate oxidase ; Drosophila pseudoobscura ; Drosophila melanogaster ; Nucleotide sequence ; Evolutionary comparison ; Gene regulation ; Malpighian tubules
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The urate oxidase (UO) transcription unit of Drosophila pseudoobscura was cloned, sequenced, and compared to the UO transcription unit from Drosophila melanogaster. In both species the UO coding region is divided into two exons of approximately equal size. The deduced D. pseudoobscura and D. melanogaster UO peptides have 346 and 352 amino acid residues, respectively. The nucleotide sequences of the D. pseudoobscura and D. melanogaster UO protein-coding regions are 82.2% identical whereas the deduced amino acid sequences are 87.6% identical with 42 amino acid changes, 33 of which occur in the first exon. Although the UO gene is expressed exclusively within the cells of the Malpighian tubules in both of these species, the temporal patterns of UO gene activity during development are markedly different. UO enzyme activity, UO protein, and UO mRNA are found in the third instar larva and adult of D. melanogaster but only in the adult stage of D. pseudoobscura. The intronic sequences and the extragenic 5′ and 3′ flanking regions of the D. pseudoobscura and D. melanogaster UO genes are highly divergent with the exception of eight small islands of conserved sequence along 772 by 5′ of the UO protein-coding region. These islands of conserved sequence are possible UO cis-acting regulatory elements as they reside along the 5′ flanking DNA of the D. melanogaster UO gene that is capable of conferring a wild-type D. melanogaster pattern of UO regulation on a UO-lacZ fusion gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00163853
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  • 2
    Electronic Resource
    Electronic Resource
    Post-receptor defect accounts for phosphorylase hypersensitivity in cultured diabetic cardiomyocytes (1992)
    Springer
    Molecular and cellular biochemistry 117 (1992), S. 63-70 
    Details
    ISSN: 1573-4919
    Keywords: glycogen phosphorylase ; alloxan-diabetes ; cardiomyocytes ; G-protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The basis for the hypersensitive response of glycogen phosphorylase to epinephrine stimulation was investigated in adult rat cardiomyocytes isolated from normal and alloxan-diabetic animals. To assess potential G-protein involvement in the response, normal and diabetic derived myocytes were incubated with either cholera or pertussis toxin prior to hormonal stimulation. Pretreatment of cardiomyocytes with cholera toxin resulted in a potentiated response to epinephrine stimulation whereas pertussis toxin did not affect the activation of this signaling pathway. To determine if the enhanced response of phosphorylase activation resulted from an alteration in adenylate cyclase activation, the cells were challenged with forskolin. After 3 hr in primary culture, diabetic cardiomyocytes exhibited a hypersensitive response to forskolin stimulation relative to normal cells. However, after 24 hr in culture, both normal and diabetic myocytes responded identically to forskolin challenge. The present data suggest that a cholera toxin sensitive G-protein mediates the hypersensitive response of glycogen phosphorylase to catecholamine stimulation in diabetic cardiomyocytes and this response which is present in alloxan-diabetic cells and is induced in vitro in normal cardiomyocytes is primarily due to a defect at a post-receptor site.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00230411
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  • 3
    Electronic Resource
    Electronic Resource
    The faint band/interband region 28C2 to 28C4-5(−) of the Drosophila melanogaster salivary gland polytene chromosomes is rich in transcripts (1991)
    Springer
    Molecular genetics and genomics 226 (1991), S. 81-87 
    Details
    ISSN: 1617-4623
    Keywords: Drosophila melanogaster ; Transcription map ; Faint bands ; Interband chromatin ; Polytene chromosomes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Urate oxidase mRNA and five other transcripts map along 38 kb of DNA in the region 28C on the Drosophila melanogaster second chromosome. Three biotinylated restriction fragments from this 38 kb of DNA, one from each end and one from the middle, were individually hybridized in situ to slightly stretched salivary gland polytene chromosomes. The data from these in situ hybridizations in combination with the transcription map of the 38 kb of DNA indicate that: (i) there are six discrete RNA species encoded along the 38 kb of DNA and (ii) these six transcripts map to the faint band/interband region which includes the proximal edge of 280, the three faint bands, 28C2, 280 and 28C4-5(−), and the adjacent interband chromatin. Our data are consistent with the few published studies directly demonstrating that faint band/interband regions of the Drosophila melanogaster salivary gland polytene chromosomes code for a high density of transcripts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00273590
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