PURIFICATION AND CHARACTERIZATION OF KANAGAWA HEMOLYSIN FROM VIBRIOPARAHAEMOLYTICUS

The haemolysin of a Kanagawa-phenomenon-positive Vibrio parahaemolyticus strain was purified to apparent homogeneity by acid precipitation, DEAE-Trisacryl, hydroxyapatite and FPLC (Mono-Q) columns: 1.4-mu-g of protein gave a single band on conventional SDS-PAGE with silver staining. The haemolysin was not inactivated by heating for 10 min at 100-degrees-C. It was a monomeric protein with a molecular weight estimated to be 29 kDa by PAGE under denaturing and non-denaturing conditions. The haemolysin caused fluid accumulation in the ligated mouse ileum, was cytolytic against cultured mammalian cells and also lysed erythrocytes of various animal species (equine erythrocytes being the most resistant).