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- W1965444911 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." @default.
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- W1965444911 date "1990-10-01" @default.
- W1965444911 modified "2023-10-16" @default.
- W1965444911 title "Gracilaria tikvahiae agglutinin. Partial purification and preliminary characterization of its carbohydrate specificity" @default.
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- W1965444911 doi "https://doi.org/10.1016/0008-6215(90)84059-4" @default.
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