Purification and characterization of an N-acetyllactosamine-specific lectin from tubers of Arum maculatum.
A lectin was purified from the tubers of Arum maculatum (family Araceae) by affinity chromatography on a thyroglobulin-Sepharose column. The lectin is not a glycoprotein and has a subunit molecular weight of 14,600. It is specifically inhibited by N-acetyllactosamine (Gal beta 1,4GlcNAc), but is not significantly inhibited by monosaccharides or by lactose (Gal beta 1,4Glc), lacto-N-biose 1 (Gal beta 1,3GlcNAc), or chitobiose (GlcNAc beta 1,4GlcNAc). Asialoglycoproteins which contain N-acetyllactosamine structures are even more effective inhibitors of the lectin. This lectin should be a useful probe for N-acetyllactosamine groups in glycoproteins.
Allen
A K
AK
Department of Biochemistry, Charing Cross and Westminster Medical School, London, UK.
D000596:Amino Acids / Q000032:analysis; D000606:Amino Sugars / Q000378:metabolism*; D000818:Animals; D006001:Glycoconjugates / Q000378:metabolism; D006388:Hemagglutinins / Q000302:isolation & purification; D006801:Humans; D037102:Lectins / Q000302:isolation & purification* / Q000378:metabolism; D019684:Magnoliopsida / Q000737:chemistry*; D037121:Plant Lectins; D011485:Protein Binding; D011817:Rabbits
D000596:Amino Acids; D000606:Amino Sugars; D006001:Glycoconjugates; D006388:Hemagglutinins; D037102:Lectins; D037121:Plant Lectins; C000458:N-acetyllactosamine