Purification and chemical characterization of antigens from sheep erythrocytes.
A mixture of glycoproteins and glycolipids was solubilized from sheep erythrocytes membranes under the effect of high ionic strength (2 M NaCl, 0.5 M Tris). Several antigenic fractions could be purified from the mixture using gel filtration on Sephadex G-200 and block electrophoresis on Pevikon C870; two fractions were found to raise antibodies in a primary reaction and these antibodies effectively sensitized erythrocytes to lysis by complement. The majority of other fractions elicited a weaker primary reaction which was detectable by both agglutination and haemolysis. The fraction, migrating fastest towards the cathode, elicited after immunization a formation of antibodies that could be detected almost exclusively by haemagglutination. The fraction, which elicited in the primary reaction a high titre of haemolytic antibodies, is composed of 72% proteins, 11% lipids and 15% saccharides.
D000818:Animals; D000906:Antibodies / Q000032:analysis; D000917:Antibody Formation; D000941:Antigens / Q000032:analysis* / Q000302:isolation & purification; D001798:Blood Proteins / Q000032:analysis; D002241:Carbohydrates / Q000032:analysis; D002850:Chromatography, Gel; D004586:Electrophoresis; D004912:Erythrocytes / Q000276:immunology*; D006386:Hemagglutination Tests; D006461:Hemolysis; D007122:Immunoelectrophoresis; D008055:Lipids / Q000032:analysis; D051379:Mice; D012756:Sheep / Q000276:immunology*
D000906:Antibodies; D000941:Antigens; D001798:Blood Proteins; D002241:Carbohydrates; D008055:Lipids