PubMed · 16632664
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R E Klaber. 2006. Phytophotodermatitis.. https://doi.org/10.1136/adc.2005.091934
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The pollen surface consists of an outermost coat and an underlying wall. It makes the initial contact with the stigma surface during sexual reproduction. To date, only two proteins have been identified from the maize pollen coat. Zea m 1 (beta-expansin 1) is the major group-1 allergen in maize pollen, but its presence and localization in the pollen coat and wall has not yet been explored. In the present study, immunoblot analysis using an antibody directed against group-1 allergen revealed that a small amount of Zea m 1 exists in the pollen coat fraction prepared using a diethyl ether wash. Immunogold labeling also showed that the extracellular localization of Zea m 1 was mainly restricted to the tectum and the foot layer of the exine (the outer pollen wall), and gold particles immunolabelling Zea m 1 were unevenly dispersed throughout the pollen coat and wall. Moreover, a substantial amount of Zea m 1 was localized in the cytoplasm of the pollen interior. The presence of Zea m 1 in the pollen coat and wall suggests that Zea m 1 may play a potential role in pollen germination on the stigma.
A combined proteomic approach was applied for the separation, identification, and comparison of two major storage proteins, beta-conglycinin and glycinin, in wild (Glycine soja) and cultivated (Glycine max) soybean seeds. Two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) with three different immobilized pH gradient (IPG) strips was an effective method to separate a large number of abundant and less-abundant storage proteins. Most of the subunits of beta-conglycinin were well-separated in the pH range 3.0-10.0, while acidic and basic glycinin polypeptides were well-separated in pH ranges 4.0-7.0 and 6.0-11.0, respectively. Although the overall distribution pattern of the protein spots was similar in both genotypes using pH 3.0-10.0, variations in number and intensity of protein spots were better resolved using a combination of pH 4.0-7.0 and pH 6.0-11.0. The total number of storage protein spots detected in wild and cultivated genotypes was approximately 44 and 34, respectively. This is the first study reporting the comparison of protein profiles of wild and cultivated genotypes of soybean seeds using proteomic tools.