Identification of the HA-2 agglutinin in the haemolymph of the ascidian Botrylloides leachii as the factor promoting adhesion of sheep erythrocytes to mouse macrophages.
The HA-2 agglutinin purified from B. leachii haemolymph is shown to mediate the binding of sheep erythrocytes to mouse macrophages. This agglutinin appears to be wholly responsible for the adhesive activity of haemolymph, since upon chromatography of the latter through Sephadex G-200, the adhesive activity for both sheep and guinea pig erythrocytes was confined to those fractions containing the HA-2 agglutinin. The HA-1 agglutinin recovered in earlier fractions was unable to promote the adhesion of guinea pig erythrocytes to macrophages. Adsorption experiments indicated that this was due to a lack of ligand sites on the macrophage surface. These data support earlier conclusions that the HA-1 and HA-2 agglutinins have distinct binding specificities.
D000818:Animals; D002122:Calcium Chloride / Q000494:pharmacology; D002448:Cell Adhesion; D004912:Erythrocytes / Q000378:metabolism*; D006168:Guinea Pigs; D006388:Hemagglutinins / Q000276:immunology* / Q000302:isolation & purification; D006458:Hemolymph / Q000032:analysis; D037102:Lectins; D008264:Macrophages / Q000378:metabolism*; D051379:Mice; D011971:Receptors, Immunologic; D012756:Sheep; D014561:Urochordata
C034185:HA-2 agglutinin; D006388:Hemagglutinins; D037102:Lectins; D011971:Receptors, Immunologic; D002122:Calcium Chloride