Characterization of the specificity of binding of Moluccella laevis lectin to glycosphingolipids

The specificity of Moluccella 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 alpha-linked N-acetylgalactosamine, b...

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Bibliographic Details
Published in:Glycoconjugate journal 1994-10, Vol.11 (5), p.418-423
Main Authors: Teneberg, S, Leonardsson, I, Angström, J, Ehrlich-Rogozinski, S, Sharon, N
Format: Article
Language:English
Subjects:
Carbohydrate Sequence
Chromatography, Affinity
Chromatography, Thin Layer
Glycosphingolipids - metabolism
Lectins - metabolism
Molecular Sequence Data
Plant Lectins
Plants - metabolism
Protein Binding
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Summary:The specificity of Moluccella 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 alpha-linked N-acetylgalactosamine, both in linear structures, as the Forssman glycosphingolipid, GalNAc alpha 3GalNAc beta 3Gal alpha 4Glc beta 1Cer, and in branched structures, as glycosphingolipids with the blood group A determinant, GalNAc alpha 3(Fuc alpha 2)Gal beta. In addition, the lectin bound, though considerably more weakly, to linear glycosphingolipids with terminal alpha-linked galactose. When considering the use of the M. laevis lectin for biochemical and medical purposes this cross-reactivity may be of importance.
ISSN:0282-0080
DOI:10.1007/BF00731277