title: Structural and functional differences of the anionic and cationic antigens in K99 extracts of Escherichia coli B41.
abstract: Radiolabelled anionic and cationic components were purified from K99 extracts of Escherichia coli B41 by immunoelectrophoresis using absorbed K99 antisera. SDS-polyacrylamide gel electrophoresis revealed that the apparent molecular weights of the polypeptide subunits were 34,000 and 19,000, respectively. Both anionic and cationic antigens in cell-free K99 extracts adhered to sheep erythrocytes after 90 min at 4 degrees C, but the cationic antigen eluted after a further 1 h at 37 degrees C. The anionic antigen did not elute from sheep erythrocytes after 18 h at 37, 43 or 56 degrees C.
mesh_terms: D000838:Anions; D000942:Antigens, Bacterial / Q000276:immunology; D000954:Antigens, Surface / Q000276:immunology; D001427:Bacterial Toxins; D002412:Cations; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000276:immunology; D004926:Escherichia coli / Q000276:immunology*; D006386:Hemagglutination Tests; D007104:Immune Adherence Reaction; D007122:Immunoelectrophoresis; D008970:Molecular Weight
chemical_list: D000838:Anions; D000942:Antigens, Bacterial; D000954:Antigens, Surface; D001427:Bacterial Toxins; D002412:Cations; C031429:K99 antigen