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  • Polyacrylamide Electrophoresis  (1)
  • sialidase  (1)
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular evolution 2 (1973), S. 339-342 
    ISSN: 1432-1432
    Keywords: Transfer-RNA ; Polyacrylamide Electrophoresis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Electrophoresis of the total transfer RNA fraction from six different sources:E. coli, brewer's yeast, wheat embryo, carp liver, rabbit liver and rat liver, was performed in a 20% polyacrylamide gel. Clear evidence was demonstrated for a decreasing tRNA size variation during evolution. Thus, two parameters seem to be involved in maintaining the necessary degree of tRNA variability: mainly tRNA size variation in lower organisms, and increased tRNA modification in higher organisms.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Glycoconjugate journal 12 (1995), S. 714-720 
    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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