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  • 1995-1999  (3)
  • 1935-1939
  • 1995  (3)
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  • 1995-1999  (3)
  • 1935-1939
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  • 1
    ISSN: 1573-4986
    Keywords: sialic acid analogues ; CMP-glycosides ; sialyltransferases ; resialylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract We present kinetic studies on the enzymatic transfer of several synthetic sialic acid analogues, modified at C-5, to distinct glycoprotein glycans by sialytransferases differing in acceptor- and linkage-specificity. Biochemical properties of sialic acids were modified by introducing formyl-, trifluoroacetyl-, benzyloxycarbonyl-, and aminoacetyl-groups to the amino group at C-5 of neuraminic acid. The latter substitution renders the corresponding α-glyocoside resistant towards sialidases. The respective CMP-sialic acid analogues were prepared by CMP-sialic acid synthase with a yield of 13–55%. The kinetic parameters of several sialyltransferases for the 5-substituted CMP-glycosides differed significantly. Relative to parent CMP-NeuAc, reaction rates of human- and rat liver Galβ1, 4GlcNAc α2,6-sialyl-transferases ranged from 50 to 170%, of GalNAc α2,6-sialyltransferases from 40–140%, and of Galβ1,3Gal-NAc α2,3-sialyltransferase from 20–50%. Resialylation of asialo-α1-acid glycoprotein by 5-N-formyl- and 5-N-aminoacetyl-neuraminic acid employing rat liver Galβ1,4GlcNAc α2,6-sialyltransferase proceeded to about 80% of galactose sites which is identical to the extent achieved with parent NeuAc. According to our data, neosialoglycoconjugates which carry sialic acids modified at theN-acetyl group can be prepared for structure-function analysis, as this position seems crucial for recognition of adhesion proteins and influenza viruses.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford [u.a.] : International Union of Crystallography (IUCr)
    Acta crystallographica 51 (1995), S. 274-277 
    ISSN: 1600-5759
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-4986
    Keywords: Anti-Pr cold agglutinins ; sialidase ; sialyltransferase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Anti-Pr cold agglutinins (CAs) with the subspecificities anti-Pr1h,-Pr1d, -Pr2, -Pr3h, -Pr3d, -PrM and anti-Sa CAs recognize immunodominantN-acetylneuraminic acid (NeuN Ac) groups of tetra and/or trisaccharides (O-glycans) of glycophorin. These O-glycans are sialylated in α2,3- and/or α2,6-linkages. Sa and most Pr antigens have been inactivated by α2,3-specific sialidases. Antigenicity was reconstituted on desialylated glycophorin by α2,3-specific Galβ1,3GalN Ac-sialyltransferase indicating that α2,3-linked NeuN Ac groups are the immunodominant components of Sa and most Pr antigens. Some Pr antigens were resistant to α2,3-specific sialidase and were not reconstituted by α2,3-specific Galβ1,3GalN Ac-sialyltransferase, which indicates that α2,6-linked NeuN Ac group represents an immunodominant component of some Pr antigens.
    Type of Medium: Electronic Resource
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