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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.
T C Chiles, and
K T Bird
May 1975,
Archives internationales de physiologie et de biochimie,
T C Chiles, and
K T Bird
March 1983,
Revista espanola de fisiologia,
T C Chiles, and
K T Bird
June 1988,
Carbohydrate research,
T C Chiles, and
K T Bird
May 2010,
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology,
T C Chiles, and
K T Bird
August 1982,
Biochimica et biophysica acta,
T C Chiles, and
K T Bird
November 1980,
Plant physiology,
T C Chiles, and
K T Bird
June 2020,
Journal of arthropod-borne diseases,
T C Chiles, and
K T Bird
April 2008,
Sheng wu gong cheng xue bao = Chinese journal of biotechnology,
T C Chiles, and
K T Bird
January 1973,
The Biochemical journal,
T C Chiles, and
K T Bird
June 1991,
Carbohydrate research,
