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  • anti-GM3-lactam and anti-GM3-lactone monoclonal IgG antibodies  (1)
  • globotriose  (1)
  • hydrogen bonds  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Anti-GM3-lactam monoclonal antibodies of the IgG type recognize natural GM3-ganglioside lactone but not GM3-ganglioside (1992)
    Springer
    Glycoconjugate journal 9 (1992), S. 303-306 
    Details
    ISSN: 1573-4986
    Keywords: anti-GM3-lactam and anti-GM3-lactone monoclonal IgG antibodies
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Immunization of mice with a synthetic GM3-lactam-BSA (bovine serum albumin) conjugate (designed to emulate the corresponding natural GM3-lactone conjugate), followed by fusion of splenocytes with myeloma cells, gave rise to more than 300 monoclonal hybridomas producing antibodies to GM3-lactam-BSA, which did not react with Glc-BSA and BSA. Eight antibody clones were randomly chosen from the positive 300 hybridomas. The eight clones, all belonging to the IgG class, were unreactive against GM3-ganglioside, whereas two antibodies (P5-1 and P5-3, both IgG1, κ) reacted with GM3-ganglioside lactone. Binding of these two antibodies to the GM3-lactam-BSA conjugate was inhibited by soluble glycosides of GM2-, GM3-, and GM4-lactam and by GM3- and GM4-lactam, respectively, but not by Gb3 or asialo-GM1 and GM2-saccharides. A third antibody (P3; IgG2b, κ) was inhibited by GM2-, GM3-, and GM4-lactam, but did not recognize GM3-ganglioside lactone.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731090
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Determination of the cell adhesion specificity of Streptococcus suis with the complete set of monodeoxy analogues of globotriose (1999)
    Springer
    Glycoconjugate journal 16 (1999), S. 67-71 
    Details
    ISSN: 1573-4986
    Keywords: bacterial adhesion ; globotriose ; monodeoxy analogues ; receptor binding ; Streptococcus suis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Streptococcus suis causes meningitis and other serious infections in pigs and humans, and binds to host cell globotriosylceramide. In order to determine the essential hydroxyls involved in binding, the complete set of monodeoxy derivatives of the receptor trisaccharide Galα1-Galβ1-4Glc were tested as inhibitors of bacterial hemagglutination. Removal of the 4″-, 6″, 2′ or 3′-hydroxyls abolished inhibitory activity, which indicated that they were critically involved in binding. The same results were obtained using synthetic lipid-linked monodeoxy derivatives of the trisaccharides in a thin-layer overlay assay. The PN and PO subtypes of the S. suis adhesin showed similar binding patterns. The hydroxyls of the glucose moiety were not critical for binding, although the adhesin binds better to the trisaccharide Galα1-4Galβ1-4Glc than the disaccharide Galα1-4Gal.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006905904544
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Synthesis, Conformational Analysis and Comparative Protein Binding of a Galabioside and Its Thioglycoside Analogues (1996)
    Weinheim : Wiley-Blackwell
    Chemistry - A European Journal 2 (1996), S. 295-302 
    Details
    ISSN: 0947-6539
    Keywords: conformational analysis ; galabioside ; hydrogen bonds ; protein recognition ; thioglycosides ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The two thio analogues (2 and 3) of TMSEt galabioside [2-(trimethylsilyl)ethyl 4-O-(α-D-galactopyranosyl)-β-D-galactopyranoside, 1], having anomeric sulfur instead of anomeric oxygen atoms, were synthesized and their conformations investigated by NMR and computational (MM 3) methods. A spacer galabioside was covalently coupled to aminated microtiter plates, and binding of a bacterial pilus adhesin (PapG) to the plates was inhibited by the soluble ligands 1, 2 and 3. The ligand 2, which has an intersaccharidic sulfur linkage, was a much less efficient inhibitor than 1, which has the natural oxygen linkage. The inhibitory power of ligand 3 was only slightly less than that of 1. An NMR experiment with 1 and 2, in which hydroxyl-group hydrogens had been partially (50%) substituted by deuterium, demonstrated the presence (in 1) and absence (in 2) of an intramolecular (HO 2′ - HO 6) hydrogen bond. This result indicates that the conformations of 1 and 2 are different and that the difference is sufficient to cause the observed (≈ 30 times) reduction of the saccharide-protein binding strength.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/chem.19960020310
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    Paper (German National Licenses)
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