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Updated: Sep 29, 2026
A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples
Published on: October 2, 2009
Specificity of Amaranthus leucocarpus lectin
E Zenteno1, R Lascurain, L F Montaño
1Departamento Biología Experimental, Universidad Autónoma del Estado de Morelos, Cuernavaca, Mexico.
We have demonstrated that Amaranthus leucocarpus lectin hemagglutinating activity was powerfully inhibited by the T-antigen, containing Gal(beta 1-3)GalNAc(alpha 1-3)Ser/Thr, and the Tn-antigen, which contains GalNAc(alpha 1-3)Ser/Thr. This suggests that the acetamido group at C-2 and the axial -OH at C-4 of the N-acetyl-D-galactopyranosylamine ring are important for lectin binding. The hemagglutination assays also established that desialylated and Pronase-treated human type O erythrocytes with an M phenotype were better recognized than erythrocytes from all other blood groups. The recognition was dependent on pH and ionic strength.
We have demonstrated that Amaranthus leucocarpus lectin hemagglutinating activity was powerfully inhibited by the T-antigen, containing Gal(beta 1-3)GalNAc(alpha 1-3)Ser/Thr, and the Tn-antigen, which contains GalNAc(alpha 1-3)Ser/Thr. This suggests that the acetamido group at C-2 and the axial -OH at C-4 of the N-acetyl-D-galactopyranosylamine ring are important for lectin binding. The hemagglutination assays also established that desialylated and Pronase-treated human type O erythrocytes with an M phenotype were better recognized than erythrocytes from all other blood groups. The recognition was dependent on pH and ionic strength.
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