The ø-haemolysin of was purified from culture supernatant fluids of type A strains fractional ammonium sulphate precipitation and isoelectric focusing in narrow pH 5 to 8 gradients. Four components detected on electrofocusing were designated ø (pI 6.8 to 6.9), ø (pI 6.5 to 6.6), ø (pI 6.1 to 6.3) and ø (pI 5.7 to 5.9). Specific activities ranged from 0.4 X 10 to 1.2 X 10 haemolytic units/mg protein and 2950 to 3600 LD/mg protein. Each haemolytic component was activated cysteine hydrochloride, and inactivated cholesterol, addition of sheep erythrocyte ghosts and heating at 60 °C for 10 min; mouse erythrocytes were more resistant than sheep erythrocytes to haemolysis. A reaction of identity was obtained between components in gel diffusion. Sodium dodecyl sulphate polyacrylamide disc gel electrophoresis gave molecular weights in the range 59000 to 62000 for each component. A similar value was obtained for ø on density gradient ultracentrifugation. Although the multiple forms were free of 11 factors present in culture supernatants, crossed immunoelectrophoresis and disc gel electrophoresis revealed minor contaminants. These studies reveal that ø-haemolysin has physical properties in common with other oxygen-labile haemolysins.


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