THE INFLUENCE OF ALPHA-GALACTOSE AND BETA-GALACTOSE RESIDUES AND SIALIC-ACID O-ACETYL GROUPS OF RAT ERYTHROCYTES ON THE INTERACTION WITH PERITONEAL-MACROPHAGES

The significance of glycoconjugates on the surface of rat erythrocytes was studied in the interaction of these cells with homologous peritoneal macrophages. The erythrocytes exposing terminal alpha-galactose and thus of B blood group specificity, as well as sialic acid are not bound by the macrophages. Beta-galactose residues exposed by sialidase induced strong binding and additional alpha-galactosidase treatment enhanced the binding. Beta-galactose exposed on glycolipids after pronase and alpha-galactosidase treatment induced no binding. An intact protein core of the glycoproteins on the erythrocyte surface was necessary for interaction with macrophages. Partial de-O-acetylation of sialic acids prior to sialidase treatment stimulated subsequent binding of the erythrocytes.