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  • 1
    Electronic Resource
    Electronic Resource
    Cell-wall proteins in pollen and roots of Lilium longiflorum: extraction and partial characterization (1983)
    Springer
    Planta 158 (1983), S. 422-427 
    Details
    ISSN: 1432-2048
    Keywords: Cell wall, proteins ; Glycoprotein (cell wall) ; Hydroxyproline-containing protein (cell wall) ; Lilium ; Pollen ; Root (cell wall)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cell-wall proteins of pollen grains, in-vitro-germinated pollen and young roots of Lilium longiflorum were studied by gel electrophoresis and amino-acid analysis. The proteins were removed from extensively purified walls by successive saline and alkali extractions. The major part including the hydroxyproline-containing proteins is covalently bound to the wall. Clear differences were observed between the proteins, especially the glycoproteins, of the pollen grain and the pollen tube. During elongation of the tubes some proteins decrease in quantity and many new proteins appear. The amount of protein in the cell walls is much lower in roots than in pollen and the root cell walls also contain fewer glycoproteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00397735
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  • 2
    Electronic Resource
    Electronic Resource
    Covalently bound wall proteins of pollen grains and pollen tubes grown in vitro and in styles after self- and cross-pollination in Lilium longiflorum (1985)
    Springer
    Theoretical and applied genetics 71 (1985), S. 263-267 
    Details
    ISSN: 1432-2242
    Keywords: Covalently bound wall proteins ; Pollen ; Pollen tubes ; Tube growth ; Incompatibility ; Lily ; Lilium longiforum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A method was worked out using trifluoromethanesulfonic acid (TFMS) as a reagent to split the covalently bound proteins, which are NaCl insoluble, from pollen tube walls of Lilium longiflorum, leaving the peptide bonds essentially intact. After electrophoretic separation, comparisons were made among these proteins from pollen grains and pollen tubes grown in vitro and in styles after self- and cross-pollination. It was found that a) the patterns of covalently bound wall proteins were different between tubes grown in vitro and in vivo; b) fewer bands were found in covalently bound wall proteins than that in noncovalently bound proteins; c) the bands remained almost the same no matter whether the tubes had been cross pollinated or self pollinated, indicating that while the noncovalently bound proteins were involved in incompatibility as shown in the previous paper, the covalently bound proteins may only serve as a structural component, having little to do with incompatibility.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00252065
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    Paper (German National Licenses)
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