Abstract
Radiolabeled anionic and cationic components were purified from K99 extracts of E. coli B41 by immunoelectrophoresis using absorbed K99 antisera. SDS[sodium dodecyl sulfate]-polyacrylamide gel electrophoresis revealed that the apparent MW 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.degree. C, but the cationic antigen eluted after a further 1 h at 37.degree. C. The anionic antigen did not elute from sheep erythrocytes after 18 h at 37, 43 or 56.degree. C.