Purification of a protein toxin from Corynebacterium ulcerans

Toxin from Corynebacterium ulcerans strain 378 was purified 66-fold by ammonium sulphate fractionation, dialysis, gel filtration on Ultrogel AcA22, ion-exchange chromatography on DEAE-cellulose and gel filtration on AcA54. On polyacrylamide-gel electrophoresis the purified material was homogeneous, staining for protein but not carbohydrate or lipid. The molecular weight of C. ulcerans toxin was 13000 as determined by SDS-polyacrylamide-gel electrophoresis and 15000 by gel filtration on AcA54.