STUDIES ON HEMOLYTIC ACTION OF A HEMOLYSIN PRODUCED BY VIBRIO-MIMICUS

Some properties and mechanism of action of a hemolysin (VMH) produced by an enteropathogenic Vibrio mimicus strain was examined. VMH was hea t-labile and inhibited by addition of divalent cations, including Ca2, Mg2+ and Mn2+. The hemolysis by VMH was inhibited by incubating with gangliosides, suggesting that the ganglioside was the binding site on the erythrocyte membrane for VMH. Existence of a galactose moiety on reducing end of the ganglioside molecule and a sialic acid on the gala ctose moiety was suggested to be important for the binding of VMH mole cule. Colloid osmotic manner of the hemolysis by VMH was demonstrated.