title: Studies on hemolytic action of a hemolysin produced by Vibrio mimicus.
abstract: Some properties and mechanism of action of a hemolysin (VMH) produced by an enteropathogenic Vibrio mimicus strain was examined. VMH was heat-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 galactose moiety was suggested to be important for the binding of VMH molecule. Colloid osmotic manner of the hemolysis by VMH was demonstrated.
authors.affiliation: Faculty of Pharmaceutical Sciences, Okayama University, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Shinoda
authors.forename: K
authors.initials: K
authors.lastname: Ishida
authors.forename: E G
authors.initials: EG
authors.lastname: Oh
authors.forename: K
authors.initials: K
authors.lastname: Sasahara
authors.forename: S
authors.initials: S
authors.lastname: Miyoshi
authors.forename: M A
authors.initials: MA
authors.lastname: Chowdhury
authors.forename: T
authors.initials: T
authors.lastname: Yasuda
mesh_terms: D000818:Animals; D001665:Binding Sites; D002240:Carbohydrate Sequence; D002412:Cations / Q000494:pharmacology; D004910:Erythrocyte Membrane / Q000378:metabolism; D004912:Erythrocytes / Q000187:drug effects; D006028:Glycosphingolipids / Q000494:pharmacology; D006460:Hemolysin Proteins / Q000096:biosynthesis / Q000494:pharmacology*; D006461:Hemolysis / Q000187:drug effects*; D006358:Hot Temperature; D006801:Humans; D008969:Molecular Sequence Data; D013696:Temperature; D014733:Vibrio / Q000378:metabolism*
chemical_list: D002412:Cations; D006028:Glycosphingolipids; D006460:Hemolysin Proteins