• Korean Journal of Fisheries and Aquatic Sciences
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• v.34 no.5
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• pp.502-508
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• 2001

The extracellualr hemolysin produced by pathogenic Vibrio furnissii was isolated and purified by ammonium sulfate precipitation and followed by DEAE-Sephadex A-50 (1st and 2nd) ion-exchange and Sephadex G-100 gel permeation chromatography. The molecular weight of the purified hemolysin was 61 kDa. The enzyme activity was inactivated by heating at 60 for 5 min, and inhibited by additions of $Cu^{2+},\;Zn^{2+}$ and a high concentration of cholesterol. Lysis of human erythrocytes by the enzyme was temperature dependent, and optimal temperature of the enzyme was $37^{\circ}C$. The purified hemolysin was unstable at pH 6.0, 6.5 and 10.0. The optimal concentration of human erythrocytes on hemolysins was about $1.5\%$. The purified hemolysin was active for erythrocytes from three animal species including mouse, rabbit and rat, and was the most active against rabbit erythrocytes. B blood group of human erythrocytes also showed a high sensitivity to the enzyme.