Gracilaria tikvahiae agglutinin. Partial purification and preliminary characterization of its carbohydrate specificity.
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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The University Hospital, Boston University Medical Center, Massachusetts 02118.
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D000373:Agglutinins / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D050260:Carbohydrate Metabolism; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002845:Chromatography / Q000379:methods; D006385:Hemagglutination Inhibition Tests; D006386:Hemagglutination Tests; D006801:Humans; D066298:In Vitro Techniques; D011817:Rabbits; D000461:Rhodophyta / Q000032:analysis*; D012756:Sheep
D000373:Agglutinins