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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1979 Jul;76(7):3358–3362. doi: 10.1073/pnas.76.7.3358

Pollen—stigma interactions: Identification and characterization of surface components with recognition potential

Adrienne Clarke *, Paul Gleeson *,, Susan Harrison *, R Bruce Knox *
PMCID: PMC383824  PMID: 16592678

Abstract

Male—female recognition in flowering plants is initiated by mutual contact of pollen and stigma surface components. Analysis of the surface macromolecules of both stigma and pollen of Gladiolus gandavensis revealed a complex mixture of proteins, glycoproteins, and glycolipids. The carbohydrate-containing components amounted to 6% in pollen and 23% in stigma and contained the monosaccharides galactose, arabinose, glucose, mannose, and rhamnose. All the mannose of both preparations was associated with a fraction that bound to concanavalin A. The stigma surface contained an arabinogalactan or arabinogalactan protein as a major component. This component has been isolated by affinity chromatography on tridacnin-Sepharose and shown to be similar in composition to a style canal component isolated in the same way. The capacity of the stigma surface preparations to bind nonspecifically to macromolecules from pollen and other sources has been demonstrated in vivo and in vitro. Specific binding of concanavalin A to the stigma surface decreases the adhesive capacity for pollen protein. The arabinogalactan of the stigma surface may act as an adhesive base. The pollen and stigma surfaces apparently complement one another to provide all the components of an ideal adhesive.

Keywords: cell surface receptors, plant glycoproteins, adhesion, concanavalin A, tridacnin

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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