PURIFICATION AND CHARACTERIZATION OF A HEMOLYSIN WITH PHOSPHOLIPASE-CACTIVITY FROM VIBRIO-CHOLERAE O139

Authors
PAL S GUHATHAKURTA B SASMAL D MALLICK R DATTA A
Citation
S. Pal et al., PURIFICATION AND CHARACTERIZATION OF A HEMOLYSIN WITH PHOSPHOLIPASE-CACTIVITY FROM VIBRIO-CHOLERAE O139, FEMS microbiology letters, 147(1), 1997, pp. 115-120
Citations number
17
Categorie Soggetti
Microbiology
Journal title
FEMS microbiology letters → ACNP
ISSN journal
03781097
Volume
147
Issue
1
Year of publication
1997
Pages
115 - 120
Database
ISI
SICI code
0378-1097(1997)147:1<115:PACOAH>2.0.ZU;2-O
Abstract
A hemolysin was purified from a Vibrio cholerae O139 strain which move d 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, suck ling mice and enhanced permeability of rabbit skin. The pi of the puri fied hemolysin was 6.4. Erythrocytes from rabbit, chicken, guinea pig, sheep and horse were sensitive to the purified hemolysin in decreasin g order of intensity. Erythrocytes from human and cow were unaffected by purified hemolysin.