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.

@article{Teneberg1994CharacterizationOB,
  title={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.},
  author={Susann Teneberg and Jonas {\AA}ngstr{\"o}m and P A Jovall and K. A. Karlsson},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 11},
  pages={8554-63}
}
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… CONTINUE READING
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