PURIFICATION AND PARTIAL IMMUNOCHEMICAL CHARACTERIZATION OF PROTEINS OF FIMBRIAE F107 FROM ESCHERICHIA-COLI ISOLATED FROM EDEMA DISEASE OF PIGS

The paper describes the isolation, purification and characterization o f F107-fimbrial proteins, obtained by thermoelution from Escherichia c oli 107/86. Isolation of the pure F107 protein was done by FPLC chroma tography, employing Superose 12, Mono Q, and Phenyl-Superose columns. The highest purity of the F107 protein was achieved with Superose 12 H R 10/30. Purity checking by a HPLC system Waters 625 LC (Millipore) pr oved the absence of protein admixtures in a fraction from Superose 12. Analysis of the molar mass of F107 proteins by SDS PAGE revealed that F107 fimbriae consist of two proteins, one of M = 43 kDa (minor), and other of M = 18.9 kDa (major). Western blot analysis with rabbit poly clonal antiserum confirmed that the 18.9 kDa protein was the major cha racteristic unit of F107 fimbriae.