Purification and characterization of thermostable direct hemolysin of Vibrio parahaemolyticus.
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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000888:Antibodies, Anti-Idiotypic; D000907:Antibodies, Bacterial / Q000302:isolation & purification*; D001322:Autoanalysis; D002241:Carbohydrates / Q000032:analysis; D002845:Chromatography; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D003911:Dextrans; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000276:immunology; D006460:Hemolysin Proteins / Q000302:isolation & purification*; D006461:Hemolysis; D006358:Hot Temperature; D006801:Humans; D007106:Immune Sera; D005779:Immunodiffusion; D008970:Molecular Weight; D010434:Pepsin A; D011817:Rabbits / Q000276:immunology; D014357:Trypsin; D014733:Vibrio / Q000276:immunology*
D000596:Amino Acids; D000888:Antibodies, Anti-Idiotypic; D000907:Antibodies, Bacterial; D002241:Carbohydrates; D003911:Dextrans; D006460:Hemolysin Proteins; D007106:Immune Sera; D014357:Trypsin; D010434:Pepsin A