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  • Drosophila melanogaster  (2)
  • Flavoprotein  (2)
  • Springer  (4)
  • 1
    ISSN: 1573-6857
    Keywords: Drosophila melanogaster ; isofemale lines ; isogroups ; natural populations ; pigmentation ; body size
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Studies of short or medium range geographic variations play an increasing role in ecological genetics, and sensitive techniques are required to detect them. In this respect, two sampling techniques were compared inD. melanogaster. The biological data were provided by the analysis of four natural populations from the same geographic area, Spain (one) and Southern France (three), for four morphometrical traits: abdomen and thoracic pigmentation, and wing and thorax lengths. Traits were measured on wild living females and on their progeny reared in the laboratory at 25°C. For progeny analyses, two techniques were compared: the usual isofemale line technique, sib families issued from a single female, and a new isogroup technique, the progeny produced by a group of 20 wild-collected parents. Large phenotypic variations were observed in wild living flies, corresponding to the unstability of natural environmental conditions during their development. Among laboratory grown flies, variations were much smaller. Between isogroups, differences were small, due to sampling error and some common environment effects. Variations between lines were much greater, thus demonstrating a strong genetic component. When different populations have to be compared, the isogroup technique should be preferred since, for the same amount of work, the lesser variability between groups provides a more precise characterization of the population means.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2048
    Keywords: l-amino-acid oxidase (molecular properties) ; Chlamydomonas (l-amino-acid oxidase) ; Flavoprotein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Anl-amino-acid oxidase (EC 1.4.3.1) that catalyzes the oxidative deamination of twelvel-amino acids has been purified 21-fold and with 14% yield to electrophoretic homogeneity fromChlamydomonas reinhardtii cells by ammonium-sulfate fractionation, gel filtration through Sephacryl and Superose, anion-exchange chromatography and preparative electrophoresis in polyacrylamide gels. The native enzyme is a protein of 470 kDa and consists of eight identical or similarsized subunits of 60 kDa each. Optimum pH and temperature were 8.2 and 55° C, respectively, with a Q10 (45–55° C) of 1.7 and an activation energy of 45 kJ · mol−1. Its absorption spectrum showed, in the visible region, maxima at 360 and 444 nm, characteristic of a flavoprotein with a calculated flavin content of 7.7 mol FAD per mol of native enzyme. ApparentK m values of the twelvel-amino acids which can act as substrates ofl-amino-acid oxidase ranged between 31 μM for phenylalanine and 176 μM for methionine. The effect of several specific group reagents, chelating agents and bivalent cations on enzyme activity has also been studied.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-2048
    Keywords: l-amino-acid oxidase (molecular properties) ; Chlamydomonas (l-amino-acid oxidase) ; Flavoprotein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An l-amino-acid oxidase (EC 1.4.3.1) that catalyzes the oxidative deamination of twelve l-amino acids has been purified 21-fold and with 14% yield to electrophoretic homogeneity from Chlamydomonas reinhardtii cells by ammonium-sulfate fractionation, gel filtration through Sephacryl and Superose, anion-exchange chromatography and preparative electrophoresis in polyacrylamide gels. The native enzyme is a protein of 470 kDa and consists of eight identical or similarsized subunits of 60 kDa each. Optimum pH and temperature were 8.2 and 55° C, respectively, with a Q10 (45–55° C) of 1.7 and an activation energy of 45 kJ · mol−1. Its absorption spectrum showed, in the visible region, maxima at 360 and 444 nm, characteristic of a flavoprotein with a calculated flavin content of 7.7 mol FAD per mol of native enzyme. Apparent K m values of the twelve l-amino acids which can act as substrates of l-amino-acid oxidase ranged between 31 μM for phenylalanine and 176 μM for methionine. The effect of several specific group reagents, chelating agents and bivalent cations on enzyme activity has also been studied.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1420-9071
    Keywords: Allozyme polymorphism ; linkage disequilibrium ; wine cellar and field populations ; Drosophila melanogaster
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Over three years, theAdh and α-Gpdh loci have been studied in two cellar populations ofDrosophila melanogaster and in two field populations which were each near to one of the cellars. Analyses of gene frequencies indicate that the divergence among subpopulations is greater in theAdh locus than in the α-Gpdh locus. Selection for or againstAdh S allele acting on theIn(2L)t inversion influences of the α-Gpdh alleles. This phenomenon may contribute to explain the maintenance of theAdh and α-Gpdh polymorphism and of theIn(2L)t inversion.
    Type of Medium: Electronic Resource
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