Isolated erythroglycans have a high-affinity interaction with wheat germ agglutinin but are poorly accessible in situ
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference33 articles.
1. Erythroglycan, a high molecular weight glycopeptide with the repeating structure [galactosyl-(1 leads to 4)-2-deoxy-2-acetamido-glucosyl(1 leads to 3)] comprising more than one-third of the protein-bound carbohydrate of human erythrocyte stroma.
2. Presence of erythroglycan on human K-562 chronic myelogenous leukemia-derived cells.
3. Studies on thyroid cell surface glycoproteins: Isolation of plasma membranes and characterization of carbohydrate units
4. Developmental change and genetic defect in the carbohydrate structure of band 3 glycoprotein of human erythrocyte membrane.
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4. Interactions of wheat-germ agglutinin with GlcNAcβ1,6Gal sequence;Biochimica et Biophysica Acta (BBA) - General Subjects;2002-01
5. A high degree of sequence homology in the putative carbohydrate recognition domains of pokeweed mitogen and wheat germ agglutinin: poly-N-acetyllactosamine-binding lectins from different species;Glycobiology;1995
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