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  • Title: Gracilaria tikvahiae agglutinin. Partial purification and preliminary characterization of its carbohydrate specificity.
    Author: Chiles TC, Bird KT.
    Journal: Carbohydr Res; 1990 Oct 25; 207(2):319-26. PubMed ID: 2076522.
    Abstract:
    A potent agglutinin of rabbit and sheep red blood cells, obtained from the red alga Gracilaria tikvahiae, was purified by ammonium sulfate fractionation, ion exchange, gel filtration, and hydroxylapatite chromatography. Human A and B blood group erythrocytes were also agglutinated, whereas human O blood group erythrocytes were not agglutinated. The hemagglutination titer was not significantly affected by the addition of EDTA or the divalent cations Ca2+, Mg2+, or Mn2+. The carbohydrate specificity was characterized by hemagglutination inhibition using various monosaccharides, glycoproteins, and glycopeptides. The results suggested that the agglutinin has affinity for N-acetylneuraminic acid as well as glycoconjugates containing N-acetylneuraminic acid.
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