Abstract
Alcian Blue proved to be a hemagglutinin specific for negatively charged receptors. Either sialylization or tryptic degradation of glycoproteins of human erythrocytes greatly diminished the agglutinability by Alcian Blue. Studies with group A antiserum, anti-AHP and the lectin of Lens culinaris demonstrated the masking efficiency of erythrocyte major glycoproteins. Previous proteolytic digestion enhanced the agglutinability of human red blood cells due to uncovering of what is considered glycolipidic group A receptors. The findings provide indirect evidence for the spatial arrangement of erythrocyte receptor sites.
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