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Theoretical and Applied Genetics

, Volume 38, Issue 8, pp 327–331 | Cite as

Disc-electrophoresis of proteins and enzymes from styles, pollen and pollen tubes of self-incompatible cultivars ofLilium longiflorum

  • Sharon Desborough
  • S. J. Peloquin
Article

Summary

Lilium longiflorum possesses several advantages for investigating the nature of self-incompatibility. The large hollow styles permit analyses of proteins and enzymes from pollen tubes removed from the styles after selfing or crossing along with their corresponding styles, as well as from pollen grains and from styles of unpollinated flowers. Biochemical methods have been developed for protein extractions and subsequent analyses by disc electrophoresis. These techniques have been used to demonstrate changing protein and esterase patterns in pollen and styles from four cultivars. No apparent association between the self-incompatibility reaction and proteins which migrate at pH 8.3 in 71/2% acryamide gel was noted. These analyses included soluble proteins, esterases, peroxidases and several dehydrogenases.

Keywords

Enzyme Electrophoresis Protein Extraction Soluble Protein Pollen Tube 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Zusammenfassung

Blüten vonLilium longiflorum bieten mehrere Vorteile bei Untersuchungen über die Natur der Selbstinkompatibilität: Die großen, hohlen Griffel lassen Protein- und Enzymanalysen sowhl von aus den Griffeln isolierten Pollen-Schläuchen nach Selbstung oder Fremdung zu, als auch von Pollen-Körnern und von bestäubten und unbestäubten Griffeln. Zur Extraktion von Proteinen und ihrer anschließenden Analyse mittels Disk-Elektrophorese wurden von uns biochemische Methoden entwickelt, die zur Demonstration von Veränderungen der Protein- und Esterase-Muster in Pollen und Griffeln von vier Klonen (cultivars) angewendet wurden. Dabei konnte kein offensichtlicher Zusammenhang zwischen der Selbstinkompatibilitätsreaktion und den bei pH 8.3 in 71/2% Acrylamid-Gel wandernden Proteinen festgestellt werden. Die Analysen erstreckten sich auf lösliche Proteine, Esterasen, Peroxydasen und eigige Dehydrogenasen.

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Copyright information

© Springer-Verlag 1968

Authors and Affiliations

  • Sharon Desborough
    • 1
  • S. J. Peloquin
    • 1
  1. 1.Departments of Genetics and HorticultureUniversity of WisconsinMadison

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