Purification and characterisation of a hemolysin with phospholipase C activity from Vibrio cholerae O139.
A hemolysin was purified from a Vibrio cholerae O139 strain which moved as a single protein band of 67 kDa in SDS-PAGE. The hemolysin showed high level of phospholipase C activity. The purified phospholipase C-hemolysin demonstrated enterotoxic activity in rabbit ileal loop, suckling mice and enhanced permeability of rabbit skin. The pI of the purified hemolysin was 6.4. Erythrocytes from rabbit, chicken, guinea pig, sheep and horse were sensitive to the purified hemolysin in decreasing order of intensity. Erythrocytes from human and cow were unaffected by purified hemolysin.
Pal
S
S
Department of Biochemistry, National Institute of Cholera and Enteric Diseases, Calcutta, India.
Guhathakurta
B
B
Sasmal
D
D
Mallick
R
R
Datta
A
A
D000818:Animals; D000833:Animals, Suckling; D001426:Bacterial Proteins / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism; D002417:Cattle; D002645:Chickens; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000382:microbiology; D006168:Guinea Pigs; D006460:Hemolysin Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D006736:Horses; D006801:Humans; D007082:Ileum / Q000382:microbiology; D051379:Mice; D011817:Rabbits; D012756:Sheep; D013696:Temperature; D013997:Time Factors; D018675:Toxicity Tests; D010738:Type C Phospholipases / Q000378:metabolism*; D014734:Vibrio cholerae / Q000737:chemistry / Q000201:enzymology*
D001426:Bacterial Proteins; D006460:Hemolysin Proteins; D010738:Type C Phospholipases