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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 4C, but the cationic antigen eluted after a further 1 h at 37 °C. The anionic antigen did not elute from sheep erythrocytes after 18 h at 37, 43 or 56 °C.
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