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

J Biol Chem. 1994 Mar 18;269(11):8554-63.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Cattle
  • Erythrina
  • Female
  • Glycolipids / chemistry*
  • Glycolipids / isolation & purification
  • Glycosphingolipids / analysis
  • Glycosphingolipids / chemistry*
  • Glycosphingolipids / isolation & purification
  • Humans
  • Lectins*
  • Magnetic Resonance Spectroscopy
  • Mass Spectrometry
  • Milk / chemistry*
  • Molecular Sequence Data
  • Plant Lectins
  • Plants, Medicinal
  • Species Specificity

Substances

  • Glycolipids
  • Glycosphingolipids
  • Lectins
  • Plant Lectins
  • erythrina lectin