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, 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.
Teneberg
S
S
Department of Medical Biochemistry and Microbiology, Göteborg University, Sweden.
Leonardsson
I
I
Angström
J
J
Ehrlich-Rogozinski
S
S
Sharon
N
N
D002240:Carbohydrate Sequence; D002846:Chromatography, Affinity; D002855:Chromatography, Thin Layer; D006028:Glycosphingolipids / Q000378:metabolism*; D037102:Lectins / Q000378:metabolism*; D008969:Molecular Sequence Data; D037121:Plant Lectins; D010944:Plants / Q000378:metabolism*; D011485:Protein Binding
D006028:Glycosphingolipids; D037102:Lectins; D037121:Plant Lectins