title: Purification and partial characterization of a Vibrio hollisae hemolysin that relates to the thermostable direct hemolysin of Vibrio parahaemolyticus.
abstract: Hemolysin produced by Vibrio hollisae (Vh-rTDH), which is related to the thermostable direct hemolysin (Vp-TDH) of Vibrio parahaemolyticus, was studied. Vh-rTDH was purified by successive column chromatographies on diethylaminoethyl-cellulose and an immunoaffinity column coupled with anti Vp-TDH immunoglobulin. The purified toxin was homogeneous, as demonstrated by conventional and sodium dodecyl sulfate--polyacrylamide gel electrophoresis (PAGE). The molecular weight of Vh-rTDH was slightly smaller than that of Vp-TDH, as determined by sodium dodecyl sulfate--slab gel electrophoresis. Conventional PAGE also showed a difference between Vh-rTDH and Vp-TDH. Vp-TDH and Vh-rTDH showed different lytic activities on erythrocytes from various animals, in particular chicken, sheep, and calf. The hemolytic activity of Vh-rTDH was heat labile when heated at 70 degrees C for 10 min, unlike Vp-TDH. Immunological cross-reactivity between Vh-rTDH and Vp-TDH was demonstrated by both the Ouchterlony test and neutralization test.
mesh_terms: D000818:Animals; D002846:Chromatography, Affinity; D006460:Hemolysin Proteins / Q000302:isolation & purification*; D006461:Hemolysis; D006801:Humans; D005779:Immunodiffusion; D009500:Neutralization Tests; D013045:Species Specificity; D014733:Vibrio / Q000276:immunology*
chemical_list: D006460:Hemolysin Proteins