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  • 1
    Electronic Resource
    Electronic Resource
    The effect of isolated components of Prunus avium L. styles on in vitro growth of pollen tubes (1982)
    Springer
    Planta 156 (1982), S. 517-519 
    Details
    ISSN: 1432-2048
    Keywords: Pollen tube growth (in vitro), inhibition ; Prunus ; S-allele ; Self-incompatibility ; Style components
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A number of components isolated from styles of P. avium cv. Napoleon (S 3 S 4) have been tested for their capacity to influence in vitro growth of pollen tubes from fresh and stored pollen (cv. Napoleon (S 3 S 4)). An antigenic glycoprotein (Antigen S) is a potent inhibitor of in-vitro pollen tube growth, causing a 65% reduction in tube length at a concentration of 20 μg/ml. None of the other style components were effective inhibitors of pollen tube growth; neither were proteins of animal origin such as histone, serum albumin, cytochrome C, and the glycoproteins ovalbumin and thyroglobulin, effective inhibitors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00392773
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    A nuclear sequence associated with self-incompatibility in Nicotiana alata has homology with mitochondrial DNA (1989)
    Springer
    Theoretical and applied genetics 77 (1989), S. 320-324 
    Details
    ISSN: 1432-2242
    Keywords: Nicotiana alata ; Self-incompatibility ; Plant mitochondrial DNA ; Interorganeller sequence transfer ; Lycopersicon
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A 1.0-kb nuclear fragment located 5′ to a coding sequence associated with self-incompatibility in N. alata shows homology with mitochondrial chromosomal DNA on Southern blots. This sequence is also present in the mitochondrial DNA of two species of tomato, L. esculentum and L. pennellii, but shows no homology to mtDNA of Zea mays. The homologous mitochondrial fragment from N. alata was cloned and sequenced. A short region of 56 bp matches the nuclear sequence in 53/56 bp. Other matched but misaligned segments flank the 3′ end. The nuclear sequence is marked at the 5′ end by two 8 bp direct repeats. The function of the nuclear sequence is not known although, it is located 397 bp upstream from the site of transcription of the self-incompatibility gene. The mitochondrial sequence contains only limited open reading frames and the nuclear sequence has none. There is evidence that additional segments of the mitochondrial clone hybridize to other nuclear sequences. The exchange of sequences between the mitochondrial and nuclear genomes of plants is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00305822
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation and partial characterization of components of Prunus avium L. styles, including an antigenic glycoprotein associated with a self-incompatibility genotype (1982)
    Springer
    Planta 156 (1982), S. 505-516 
    Details
    ISSN: 1432-2048
    Keywords: Antigen ; Glycoprotein ; Pollination ; Prunus ; S-allele ; Self-incompatibility ; Style mucilage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Several components of buffer extracts of Prunus avium L. styles (cv. Lambert, S 3 S 4) have been isolated and partially characterized: the major component is a glycoprotein (molecular weight approx. 90,000; 95% protein, 5.4% carbohydrate). A “sticky” uronic-acid-containing component and an arabinogalactan are also present. Two minor components are an antigenic glycoprotein associated with the self-incompatibility genotype (Antigen S) and a component found in styles of all Prunus species (Antigen P). The isolated glycoproteins have a substantial carbohydrate content (Antigen P 17.2%; Antigen S 16.3%), and have apparent molecular weights of 32,000 (Antigen P) and 37,000–39,000 (Antigen S). They are antigenically quite distinct. Material corresponding to Antigen S is secreted into the medium of suspension-cultured callus cells raised from both leaf and stem of P. avium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00392772
    Location Call Number Limitation Availability
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    Paper (German National Licenses)
    Fulltext
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