Characterization of binding of Gal beta 4GlcNAc-specific lectins from Erythrina cristagalli and Erythrina corallodendron to glycosphinogolipids. Detection, isolation, and characterization of a novel glycosphinglipid of bovine buttermilk.
The lectins from seeds of Erythrina cristagalli and Erythrina corallodendron were characterized for binding to glycolipids, using a chromatogram binding assay, a microtiter well assay, and glycolipids coated on erythrocytes. Both lectins bound to glycolipids having a terminal Gal beta 4GlcNAc sequence and also, with similar affinity, to glycolipids with terminal Fuc alpha 2Gal beta 4GlcNAc (blood group H determinant on a type 2 chain). All other substitutions of Gal beta 4GlcNAc tested abolished the binding. A binding epitope for the Erythrina lectins was considered by comparison of minimum energy conformations of binding and nonbinding glycolipids. A non-acid glycolipid, with lectin binding activity, was found in bovine buttermilk. By mass spectrometry and proton NMR spectroscopy it was shown to be a branched hexaglycosylceramide with the structure Gal beta 4Glc-NAc beta 6(Gal beta 4GlcNAc beta 3)Gal beta 4Glc beta Cer. This glycosphingolipid has not been reported before.
Teneberg
S
S
Department of Medical Biochemistry, University of Göteborg, Sweden.
Angström
J
J
Jovall
P A
PA
Karlsson
K A
KA
D000818:Animals; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002417:Cattle; D004895:Erythrina; D005260:Female; D006017:Glycolipids / Q000737:chemistry* / Q000302:isolation & purification; D006028:Glycosphingolipids / Q000032:analysis / Q000737:chemistry* / Q000302:isolation & purification; D006801:Humans; D037102:Lectins; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D008892:Milk / Q000737:chemistry*; D008969:Molecular Sequence Data; D037121:Plant Lectins; D010946:Plants, Medicinal; D013045:Species Specificity
D006017:Glycolipids; D006028:Glycosphingolipids; D037102:Lectins; D037121:Plant Lectins; C045629:erythrina lectin