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  • Computational Chemistry and Molecular Modeling  (3)
  • Drosophila melanogaster  (3)
  • 1
    Digitale Medien
    Digitale Medien
    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
    Schlagwort(e): Urate oxidase ; Drosophila pseudoobscura ; Drosophila melanogaster ; Nucleotide sequence ; Evolutionary comparison ; Gene regulation ; Malpighian tubules
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00163853
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  • 2
    Digitale Medien
    Digitale Medien
    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
    Schlagwort(e): Drosophila melanogaster ; Transcription map ; Faint bands ; Interband chromatin ; Polytene chromosomes
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00273590
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  • 3
    Digitale Medien
    Digitale Medien
    Errata (1973)
    New York, NY : Wiley-Blackwell
    International Journal of Quantum Chemistry 7 (1973), S. 635-636 
    Details
    ISSN: 0020-7608
    Schlagwort(e): Computational Chemistry and Molecular Modeling ; Atomic, Molecular and Optical Physics
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Zusätzliches Material: 1 Tab.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/qua.560070316
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  • 4
    Digitale Medien
    Digitale Medien
    Theoretical studies of diamagnetic properties of the hydrogen molecule ion. I. Approximate variation-perturbation calculation (1972)
    New York, NY : Wiley-Blackwell
    International Journal of Quantum Chemistry 6 (1972), S. 651-661 
    Details
    ISSN: 0020-7608
    Schlagwort(e): Computational Chemistry and Molecular Modeling ; Atomic, Molecular and Optical Physics
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: A variation-perturbation method, analogous to a technique devised by Das and Bersohn for the study of the hydrogen molecule, is developed for calculation of the diamagnetic susceptibility χ and magnetic shielding σ and is applied to a study of the hydrogen molecule ion. Two approximations are investigated-in a first approximation, χ = -0.37814α2ao3 and σ = 1.112 × 10-5 c.g.s. units and in a second approximation, χ = -0.37569α2ao3 and σ = 1.128 × 10-5 c.g.s. units.
    Zusätzliches Material: 1 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/qua.560060409
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  • 5
    Digitale Medien
    Digitale Medien
    Theoretical studies of diamagnetic properties of the hydrogen molecule ion II. Effect of varying internuclear separation (1972)
    New York, NY : Wiley-Blackwell
    International Journal of Quantum Chemistry 6 (1972), S. 663-668 
    Details
    ISSN: 0020-7608
    Schlagwort(e): Computational Chemistry and Molecular Modeling ; Atomic, Molecular and Optical Physics
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: The diamagnetic susceptibility χ and magnetic shielding σ for H2+ are investigated in the range of internuclear separations R = 1.6 a.u. to R = 2.4 a.u. according to a previously reported technique. From this data values of 〈χ〉 and 〈σ〉, for which nuclear motion due to zero-point vibration and centrifugal stretching is taken into account, are calculated at 300°K. These averages are 〈χ〉 = -0.3902 α2ao3 and 〈σ〉 = 1.096 × 10-5 c.g.s. units which are approximately 3.1% and 1.4% respectively, smaller than the equilibrium values.
    Zusätzliches Material: 3 Tab.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/qua.560060410
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  • 6
    Digitale Medien
    Digitale Medien
    Temporal control of urate oxidase activity during development of the third-instar larva of Drosophila: The role of 20-hydroxyecdysone (1982)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 3 (1982), S. 215-233 
    Details
    ISSN: 0192-253X
    Schlagwort(e): urate oxidase ; 20-hydroxyecdysone ; Drosophila melanogaster ; Malpighian tubules ; Life and Medical Sciences ; Genetics
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie
    Notizen: 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.
    Zusätzliches Material: 8 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/dvg.1020030305
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