TY - JOUR
T1 - Some Properties of Vibrio vulnificus Hemolysin
AU - Shinoda, Sumio
AU - Miyoshi, Shin Ichi
AU - Yamanaka, Hiroyasu
AU - Miyoshi-Nakahara, Noriko
PY - 1985
Y1 - 1985
N2 - 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.
AB - 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.
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U2 - 10.1111/j.1348-0421.1985.tb00862.x
DO - 10.1111/j.1348-0421.1985.tb00862.x
M3 - Article
C2 - 4088099
AN - SCOPUS:0022255540
VL - 29
SP - 583
EP - 590
JO - Microbiology and Immunology
JF - Microbiology and Immunology
SN - 0385-5600
IS - 7
ER -