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Infect Immun. 1973 November; 8(5): 775-780
Copyright © 1973 American Society for Microbiology. All Rights Reserved.

Purification and Characterization of Thermostable Direct Hemolysin of Vibrio parahaemolyticus

Department of Bacteriology and Serology, Research Institute for Microbial Diseases, Osaka University, Yamada-Kami, Suita, Osaka, Japan

ABSTRACT

A thermostable direct hemolysin was purified from culture filtrates of Vibrio parahaemolyticus. The purified hemolysin gave one precipitation line with the antihemolysin antiserum on agar-gel diffusion test and a single band on polyacrylamide gel electrophoresis. The hemolysin was not inactivated by heating at 70 to 100 C for 10 min. The hemolytic activity was not enhanced by the addition of lecithin. It was demonstrated that the hemolysin was a protein with a molecular weight of approximately 118,000. Amino acid analysis revealed that 43% of total amino acids were acidic amino acids, whereas 11% were basic amino acids.

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