Some properties of he nolysin produced by Vibrio vulnificus were investi-gated. The hemolysin was heat labile, and the hemolytic activity was inhibited by adding cholesterol or divalent cations. Cholesterol inhibited the temperature-inde-pendent hemolysin-binding step, suggesting that cholesterol made up the binding site of the cell membrane, whereas the divalent cations inhibited the temperature-depend-ent membrane-degradation step. However, the V. vulnificus hemolysin was stable to oxygen and sulfhydryl reagents and was not inactivated by antiserum against strepto-lysin O, suggesting that the V. vulnificus hemolysin differs from oxygen-labile hemo-lysins which bind to cholesterol. Tne V. vulnificus hemolysin seerrs to be one of the exceptional cholesterol-binding hemolysins.
|Number of pages||8|
|Journal||MICROBIOLOGY and IMMUNOLOGY|
|Publication status||Published - 1985|
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