Asparagine-linked oligosaccharides containing poly-N-acetyllactosamine chains are preferentially bound by immobilized calf heart agglutinin.
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.
Merkle
R K
RK
Department of Biochemistry, School of Chemical Sciences, University of Georgia, Athens 30602.
Cummings
R D
RD
D000818:Animals; D001216:Asparagine; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002460:Cell Line; D002846:Chromatography, Affinity; D037161:Galectins; D006020:Glycopeptides / Q000302:isolation & purification / Q000378:metabolism; D006388:Hemagglutinins / Q000378:metabolism*; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000302:isolation & purification / Q000378:metabolism*; D011134:Polysaccharides
D037161:Galectins; D006020:Glycopeptides; D006388:Hemagglutinins; D009844:Oligosaccharides; D011134:Polysaccharides; D001216:Asparagine; C037199:poly-N-acetyllactosamine