Glycoconjugate Journal

, Volume 11, Issue 5, pp 418–423 | Cite as

Characterization of the specificity of binding ofMoluccella laevis lectin to glycosphingolipids

  • Susann Teneberg
  • Iréne Leonardsson
  • Jonas Ångström
  • Sarah Ehrlich-Rogozinski
  • Nathan Sharon
Lectin Papers


The specificity ofMoluccella laevis lectin was investigated by analysing its binding to glycosphingolipids separated on thin-layer chromatograms or adsorbed on microtitre wells. The binding activity of the lectin was highest for glycosphingolipids with terminal α-linkedN-acetylgalactosamine, both in linear structures, as the Forssman glycosphingolipid, GalNAcα3GalNAcβ3Galα4Galβ4Glcβ1Cer, and in branched structures, as glycosphingolipids with the blood group A determinant, GalNAcα3(Fucα2)Galβ. In addition, the lectin bound, though considerably more weakly, to linear glycosphingolipids with terminal α-linked galactose. When considering the use of theM. laevis lectin for biochemical and medical purposes this cross-reactivity may be of importance.


Moluccella laevis lectin glycosphingolipid N-acetylgalactosamine 


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Copyright information

© Chapman & Hall 1994

Authors and Affiliations

  • Susann Teneberg
    • 1
  • Iréne Leonardsson
    • 1
  • Jonas Ångström
    • 1
  • Sarah Ehrlich-Rogozinski
    • 2
  • Nathan Sharon
    • 2
  1. 1.Department of Medical Biochemistry and MicrobiologyGöteborg UniversityGöteborgSweden
  2. 2.Department of Membrane Research and BiophysicsThe Weizmann InstituteRehovotIsrael

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