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      Asparagine-linked oligosaccharides containing poly-N-acetyllactosamine chains are preferentially bound by immobilized calf heart agglutinin.

      The Journal of Biological Chemistry
      Animals, Asparagine, Carbohydrate Conformation, Carbohydrate Sequence, Cell Line, Chromatography, Affinity, Galectins, Glycopeptides, isolation & purification, metabolism, Hemagglutinins, Molecular Sequence Data, Oligosaccharides, Polysaccharides

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          Abstract

          We have investigated the carbohydrate-binding specificity of a mammalian lectin, calf heart agglutinin, by determining the interaction of the immobilized lectin with a variety of complex-type Asn-linked oligosaccharides. Our results demonstrate that calf-heart agglutinin binds with high affinity to oligosaccharides containing the repeating disaccharide (3Gal beta 1-4GlcNAc beta 1)n or poly-N-acetyllactosamine sequence and that the presence of terminal beta-linked galactosyl residues is neither sufficient nor necessary for high affinity interactions.

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