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  • 1975-1979  (2)
  • Colias  (2)
  • 1
    Digitale Medien
    Digitale Medien
    Polymorphism and predictability at the α-glycerophosphate dehydrogenase locus in Colias butterflies: Gradients in allele frequency within single populations (1976)
    Springer
    Biochemical genetics 14 (1976), S. 403-426 
    Details
    ISSN: 1573-4927
    Schlagwort(e): polymorphism ; Colias ; α-glycerophosphate dehydrogenase ; cline
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Abstract Heterozygosity at the α-glycerophosphate dehydrogenase locus of five species of Colias butterflies is widespread in montane populations; alpine and lowland populations are not heterozygous. Within a single demographically characterized population of C. meadii where the population extends from alpine down into montane habitats, a marked cline in allele frequency is seen. Such within-population clines suggest the involvement of strong selection across the marked ecological interface. Thermal factors are the most likely causative agents, but associative overdominance is not excluded.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00486123
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Characterization of electrophoretically cryptic variation in the alpine butterfly Colias meadii (1977)
    Springer
    Biochemical genetics 15 (1977), S. 665-693 
    Details
    ISSN: 1573-4927
    Schlagwort(e): Colias ; enzyme polymorphism ; protein conformation ; electrophoresis
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Abstract Enzyme polymorphism was characterized among the proteins of 14 loci of Coliae meadii by replicate electrophoresis in polyacrylamide gels of differing pore size. The results reveal a large number of variants, with a very skewed frequency distribution. A large fraction of the variants cannot be differentiated by electrophoresis in 5–7% acrylamide gels. This gel sieving approach permits an estimate of the relative contributions of charge and of conformation to electrophoretic mobility. Many of the variant proteins do not differ in charge. Most variants exhibit different degrees of interaction with the gel and presumably differ in conformation.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00484097
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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    Artikel (Nationallizenzen)
    Volltext
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