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  • 1
    Electronic Resource
    Electronic Resource
    The nature of callose produced during self-pollination inSecale cereale (1980)
    Springer
    Planta 148 (1980), S. 498-509 
    Details
    ISSN: 1432-2048
    Keywords: Callose ; Pollination ; Secale ; Self-incompatibility
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The response to incompatible (self) pollination in rye (Secale cereale L.) includes the rapid deposition in the germinating pollen grain and pollen tube of a substance that stains with aniline blue, resorcin blue and calcofluor, and in these respects resembles callose. This substance has been isolated and analysed by acid hydrolysis and methylation as well as specific enzyme hydrolysis. It contains a glucan component with 1,4-β-glucosidic and 1,3-β-glucosidic linkages within the same linear chains. The proportion of 1,4-to 1,3-glucosidic linkages in the preparation is 77∶9.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02395321
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The nature of callose produced during self-pollination inSecale cereale (1980)
    Springer
    Planta 148 (1980), S. 498-509 
    Details
    ISSN: 1432-2048
    Keywords: Callose ; Pollination ; Secale ; Self-incompatibility
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The response to incompatible (self) pollination in rye (Secale cereale L.) includes the rapid deposition in the germinating pollen grain and pollen tube of a substance that stains with aniline blue, resorcin blue and calcofluor, and in these respects resembles callose. This substance has been isolated and analysed by acid hydrolysis and methylation as well as specific enzyme hydrolysis. It contains a glucan component with 1,4-β-glucosidic and 1,3-β-glucosidic linkages within the same linear chains. The proportion of 1,4-to 1,3-glucosidic linkages in the preparation is 77∶9.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00552666
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Style antigens of Prunus avium L. (1981)
    Springer
    Planta 153 (1981), S. 125-129 
    Details
    ISSN: 1432-2048
    Keywords: Antigen (style) ; Prunus ; Self-incompatibility ; Style antigens
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Antiserum to a protein fraction of an extract of mature styles of P. avium cv. Lambert (S 3 S 4) was raised in rabbits. Two major antigenic components of the style extracts were detected by immunoelectrophoresis and immunodiffusion. The presence of one antigen (S-antigen) correlated with a particular S-genotype (S 3 S 4). This antigen is restricted to mature styles of P. avium. The second antigen (P-antigen) was detected in styles of all Prunus species examined, but not in styles of other species of the Rosaceae. The S-antigen is positively charged and the P-antigen negatively charged at pH 8.8.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00384093
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  • 4
    Electronic Resource
    Electronic Resource
    Tissue-specific antigens secreted by suspension-cultured callus cells of Prunus avium L. (1981)
    Springer
    Planta 153 (1981), S. 115-124 
    Details
    ISSN: 1432-2048
    Keywords: Antigen ; Callus ; Cell suspension culture ; Prunus ; Rosaceae ; Secretions, extracellular ; Self-incompatibility
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A number of antigenic components are secreted into the medium by P. avium callus cells derived from different tissues and grown in suspension culture. These antigens have been detected using antiserum raised in rabbits to a protein fraction secreted by P. avium leaf callus. One antigen is specific to leaf tissue and is secreted by callus cells derived from stem, pistil and anthers as well as leaves. A second antigen is, in intact organs, restricted to styles of a particular self-incompatibility (S) genotype, but is also secreted by callus cells derived from the leaf. Another antigen, apparently not organ-specific, is secreted by all calli tested, including Rosa (cv. Paul's Scarlet).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00384092
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  • 5
    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
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  • 6
    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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  • 7
    Electronic Resource
    Electronic Resource
    Self-compatibility in aLycopersicon peruvianum variant (LA2157) is associated with a lack of style S-RNase activity (1994)
    Springer
    Theoretical and applied genetics 88 (1994), S. 859-864 
    Details
    ISSN: 1432-2242
    Keywords: Tomato ; Lycopersicon peruvianum ; Self-incompatibility ; S-locus mutation ; Pollination Style-ribonuclease (S-RNase)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A series of crosses between a naturally-occurring self-compatible accession ofLycopersicon peruvianum and a closely-related self-incompatible accession were used to demonstrate that the mutation to self-compatibility is located at the S-locus. Progeny of the crosses contain abundant style proteins of about 30 kDa that segregate with the S6and S7-alleles from the SI parent and the Sc-allele from the SC parent. The S6and S7-associated proteins have ribonuclease activity whereas the Sc-associated protein is not an active ribonuclease. This finding indicates that S-RNases are determinants of self-incompatibility in the style and that the ribonuclease activity is essential for their function.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01253997
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  • 8
    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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  • 9
    Electronic Resource
    Electronic Resource
    A style-specific 120-kDa glycoprotein enters pollen tubes of Nicotiana alata in vivo (1996)
    Springer
    Sexual plant reproduction 9 (1996), S. 75-86 
    Details
    ISSN: 1432-2145
    Keywords: Key words Hydroxyproline-rich glycoprotein ; Pistil ; Pollen tubes ; Self-incompatibility
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Pistils of Nicotiana alata (Link et Otto) contain an abundant, style-specific glycoprotein (120 kDa) that is rich in hydroxyproline and has both extensin-like and arabinogalactan-protein-like carbohydrate substituents. An antibody specific for the protein backbone of the glycoprotein was used to localise the glycoprotein in both unpollinated and pollinated pistils. The glycoprotein is evenly distributed in the extracellular matrix of the style transmitting tract of unpollinated pistils and, despite the presence of extensin-like carbohydrate substituents, is not associated with the walls of the transmitting tract cells. In pollinated pistils the 120-kDa glycoprotein is concentrated in the extracellular matrix adjacent to pollen tubes, and is also present in the cytoplasm and the cell walls of pollen tubes. Pollen tubes grown in vitro do not contain the 120-kDa glycoprotein unless it is added to the growth medium, suggesting that the 120-kDa glycoprotein located in pistil-grown pollen tubes is derived from the extracellular matrix of the transmitting tract.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004970050013
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