- Identification of hemolysin as one of the important virulent factors in vibrio anguillarum V7
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Choe, Young Chool , Jeong, Ga Jin
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J. Microbiol. 1995;33(4):283-288.
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Abstract
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We have identified hemolysin rendering virulency of Vibrio anguilarum grown at 23℃ which was evaluated on human RBCs. Hemolysin itself was separated as a single band on non-denaturing gel electrophoresis. Vibrio hemolysin was destroyed by trypsin and proteinase K and was heat labile. Optimal pH for activity was around pH 6 while pI of the molecule was recognized as 5.7, with relative distance (R_f) on non-denaturing gel was 0.7. Addition of EDTA and FeCI₃drew the possibility that the production of hemolysin was mainly induced to overcome iron deficiency inside host animals upon infection.
- Physiological characterization of kinetics and action mechanism of vibrio hemolysin
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Choe, Young Chool , Jeong, Ga Jin
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J. Microbiol. 1995;33(4):289-294.
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Abstract
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The action mechanism of hemolysin rendering virulency of Vibrio anguilarum has not clarified as yet, even though there were several possible factors explained. We have studied hemolytic kinetics performed by hemolysin from V. anguillarum strain V7 as well as binding of hemolysin to RBC membrane. Maximal rate of hemolysis and duration of lag phase were directly and inversly correlated to the concentration of hemolysin used. Hemolysin molecules are known to bind consumptively with proper diameter, while other protectants with smaller diameter could not. In conclusion, hemolysin should bind irreversibly to RBC membrane exert hemolysis distorting osmotic pressure. The binding could be hindered by spatial structure of the RBC surfacem which might be caused by sialic acid.
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