title: A haemagglutinin in the tissue fluid of the Pacific oyster, Crassostrea gigas, with specificity for sialic acid residues in glycoproteins.
abstract: An agglutinin for human red cells has a specificity for sialic acid and a high affinity for bovine salivary glycoprotein. Digestion of the glycoprotein with Pronase or neuraminidas indicated that binding of sialic acid to receptors in the agglutinin is the first step in the mechanism of formation of a stable complex between ligand and receptor.
mesh_terms: D000373:Agglutinins / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D004910:Erythrocyte Membrane / Q000378:metabolism; D005732:Gangliosides / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism*; D006388:Hemagglutinins / Q000302:isolation & purification / Q000378:metabolism*; D006458:Hemolymph / Q000032:analysis; D006736:Horses; D006801:Humans; D010125:Ostreidae / Q000032:analysis*; D012794:Sialic Acids / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D000373:Agglutinins; D005732:Gangliosides; D006023:Glycoproteins; D006388:Hemagglutinins; D012794:Sialic Acids