Purification and characterization of Kanagawa haemolysin from Vibrio parahaemolyticus.
The haemolysin of a Kanagawa-phenomenon-positive Vibrio parahaemolyticus strain was purified to apparent homogeneity by acid precipitation, DEAE-Trisacryl, hydroxyapatite and FPLC (Mono-Q) columns: 1.4 micrograms of protein gave a single band on conventional SDS-PAGE with silver staining. The haemolysin was not inactivated by heating for 10 min at 100 degrees C. It was a monomeric protein with a molecular weight estimated to be 29 kDa by PAGE under denaturing and non-denaturing conditions. The haemolysin caused fluid accumulation in the ligated mouse ileum, was cytolytic against cultured mammalian cells and also lysed erythrocytes of various animal species (equine erythrocytes being the most resistant).
Douet
J P
JP
Université de Bordeaux I, Talence, France.
Castroviejo
M
M
Dodin
A
A
Bébéar
C
C
D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D006460:Hemolysin Proteins / Q000302:isolation & purification* / Q000378:metabolism; D006358:Hot Temperature; D066298:In Vitro Techniques; D008970:Molecular Weight; D010449:Peptide Mapping; D014736:Vibrio parahaemolyticus / Q000378:metabolism*
D006460:Hemolysin Proteins