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  • 1
    Electronic Resource
    Electronic Resource
    New cleavable photoreactive heterobifunctional cross linking reagents for studying membrane organization (1980)
    s.l. : American Chemical Society
    Biochemistry 19 (1980), S. 4423-4429 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00560a007
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  • 2
    Electronic Resource
    Electronic Resource
    Effect of Candida albicans cell wall components on the adhesion of the fungus to human and murine vaginal mucosa (1988)
    Springer
    Mycopathologia 102 (1988), S. 115-121 
    Details
    ISSN: 1573-0832
    Keywords: C. albicans adherence ; vaginal mucosa
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract In this study, cell walls from Candida albicans were separated and chitin was isolated from these cell walls. A chitin soluble extract (CSE) prepared from the chitin inhibited in vitro adhesion of C. albicans to human epithelial vaginal cells (VEC), and blocked in vivo attachment to murine vaginal mucosa, thereby preventing candidal infection in these animals. These findings suggest that the CSE acts as an adhesin-like substance. Fractionation of CSE yielded two fractions: FI and FII, of which only FI exhibited inhibitory activity. Chemical analysis of CSE and its two fractions revealed that CSE contains over 70% of proteins, most of which were found in the non-active fraction. In addition, 3% of amino-sugars were found in the FI active fraction. Lipids were also detected in the unfractionated CSE and in both fractions. Experiments to further characterize the component(s) in the CSE inhibiting the attachment of C. albicans are in progress in our laboratory.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00437448
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  • 3
    Electronic Resource
    Electronic Resource
    Lectin biochemistry: New way of protein maturation (1986)
    [s.l.] : Nature Publishing Group
    Nature 323 (1986), S. 203-204 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] WHEN last year it was claimed that the mature form of the jack bean lectin con-canavalin A (Con A) is made by the breakage and rejoining of its precursor peptide1, some scepticism was voiced in a News and Views article2. This was not surprising as a novel form of protein maturation had been ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/323203a0
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  • 4
    Electronic Resource
    Electronic Resource
    Distribution of lectins in membranes of soybean and peanut plants (1979)
    Springer
    Planta 145 (1979), S. 193-198 
    Details
    ISSN: 1432-2048
    Keywords: Lectins ; Membranes ; Peanut ; Soybean
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The distribution of lectin activity in soybean and peanut plants has been investigated. In both plants activity is found in all tissues examined (roots, shoots and leaves) at all stages of development from seedling to maturity (7 weeks). The cellular location of the lectins differs between soybean and peanut: in soybean the lectins are generally membrane-associated, whereas in peanut plants lectin activity is present also in the soluble cytoplasmic fraction. The membrane-associated lectins appear to differ from the seed lectins of the respective plants. The function of membrane-associated lectins is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00388717
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  • 5
    Electronic Resource
    Electronic Resource
    Different locations of carbohydrate-containing sites in the surface membrane of normal and transformed mammalian cells (1970)
    Springer
    The journal of membrane biology 3 (1970), S. 267-279 
    Details
    ISSN: 1432-1424
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A soybean agglutinin was found to agglutinate mouse, rat and human cell lines transformed by viral carcinogens, but not hamster cells transformed by viral or non-viral carcinogens. Normal cells from which the transformed cells were derived were not agglutinated by this agglutinin, but they were rendered agglutinable after short incubation with trypsin or pronase. The transformed hamster cells, on the other hand, became agglutinable only after prolonged treatment with pronase. The agglutination was specifically inhibited by N-acetyl-d-galactosamine, indicating that N-acetyl-d-galactosamine-like saccharides are part of the receptor sites for soybean agglutinin on the surface membrane. Such sites exist in a cryptic form in normal cells; they are exposed in transformed mouse, rat and human cells, but become less accessible in transformed hamster cells. The receptor sites for soybean agglutinin differ from the receptors for two other plant agglutinins (wheat germ agglutinin that interacts with N-acetyl-d-glucosamine-like sites and Concanavalin A that interacts with α-d-glucopyranoside-like sites) which become exposed upon transformation of all lines tested. In normal hamster cells, the receptors for all three agglutinins become exposed after incubation with trypsin, but the exposure of N-acetyl-d-galactosamine-like sites requires the longest enzyme treatment. The results indicate a difference in the location of different carbohydrate-containing sites in the surface membrane. The differences in the exposure of carbohydrate-containing sites in the membrane could not be correlated with the levels of carbohydrate-splitting glycosidases in normal and transformed cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01868019
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  • 6
    Electronic Resource
    Electronic Resource
    The structure of the erythrina corallodendron lectin at 2.0 Å resolution: What does it tell us about protein-carbohydrate interactions? (1992)
    Springer
    Fresenius' Zeitschrift für analytische Chemie 343 (1992), S. 43-43 
    Details
    ISSN: 1618-2650
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00331986
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  • 7
    Electronic Resource
    Electronic Resource
    The glycolipid specificity ofErythrina cristagalli agglutinin (1987)
    Springer
    Glycoconjugate journal 4 (1987), S. 379-390 
    Details
    ISSN: 1573-4986
    Keywords: Erythrina cristagalli ; lectins ; glycolipids ; para-globoside
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The interaction of125I-labeledErythrina cristagalli agglutinin (ECA) with neutral glycosphingolipids on thin layer chromatograms was examined by the overlay technique followed by radioautography. The lectin bound topara-globoside with a sensitivity about 10 times higher than to lactosylceramide or globoside, in agreement with the specificity of the lectin forN-acetyllactosamine. The lower limit of detection ofpara-globoside was about 0.66 nmol. The specific binding of ECA to this glycolipid was confirmed by a highly sensitive enzyme-linked lectin assay (ELLA), utilizing the horseradish peroxidase-avidin-biotin system for detection of bound lectin. Overlays of neutral glycosphingolipid extracts from human erythrocyte membranes and from human granulocytes with ECA demonstrated that the lectin can be employed for the detection of small amounts ofpara-globoside in biological materials also in the presence of excess globoside. No staining was obtained when thin layer chromatograms of neutral glycosphingolipid extracts from rabbit erythrocyte membranes were overlayed with125I-ECA. Afterin situ treatment of the chromatograms with α-galactosidase, the lectin bound to several components, one of which had a mobility corresponding to that of the pentahexosylceramide Galα3Galβ4GlcNAcβ3Galβ4Glcβ1Cer, the major neutral glycosphingolipid of rabbit erythrocytes, thus providing further evidence for the specificity of ECA forpara-globoside.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01048371
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  • 8
    Electronic Resource
    Electronic Resource
    Binding and precipitating activities ofErythrina lectins with complex type carbohydrates and synthetic cluster glycosides. A comparative study of the lectins fromE. corallodendron, E. cristagalli, E. flabelliformis, andE. indica (1989)
    Springer
    Glycoconjugate journal 6 (1989), S. 141-150 
    Details
    ISSN: 1573-4986
    Keywords: Erythrina lectins ; complex type carbohydrates ; cluster glycosides ; binding and precipitation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Erythrina lectins possess similar structural and carbohydrate binding properties. Recently, tri- and tetra-antennary complex type carbohydrates with non-reducing terminal galactose residues have been shown to be precipitated as tri- and tetravalent ligands, respectively, with certainErythrina lectins [Bhattacharyya L, Haraldsson M, Brewer CF (1988) Biochemistry 27∶1034-41]. The present work describes a comparative study of the binding and precipitating activities of fourErythrina lectins,viz. E. corallodendron, E. cristagalli, E. flabelliformis, andE. indica, with multi-antennary complex type carbohydrates and synthetic cluster glycosides. The results show that though their binding affinities are very similar, theErythrina lectins show large differences in their precipitating activities with the carbohydrates. The results also indicate significant dependence of the precipitating activities of the lectins on the core structure of the carbohydrates. These findings provide a new dimension to the structure-activity relationship of the lectins and their interactions with asparagine-linked carbohydrates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01047896
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