Purification and Characterization of Thermostable Direct Hemolysin of Vibrio parahaemolyticus

AUTOR(ES)

Sakurai, Jun

RESUMO

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.

Documentos Relacionados

• Purification and partial characterization of a non-O1 Vibrio cholerae hemolysin that cross-reacts with thermostable direct hemolysin of Vibrio parahaemolyticus.
• Purification and characterization of a hemolysin produced by a clinical isolate of Kanagawa phenomenon-negative Vibrio parahaemolyticus and related to the thermostable direct hemolysin.
• Enterotoxigenicity of Vibrio parahaemolyticus with and without genes encoding thermostable direct hemolysin.
• Nucleotide sequence of the thermostable direct hemolysin gene of Vibrio parahaemolyticus.
• Characterization of the temperature-dependent inactivating factor of the thermostable direct hemolysin in Vibrio parahaemolyticus.