The hydrophobic character of thiol-activated cytolysins.
Hydrophobic chromatography on phenyl-Sepharose has revealed the decidedly hydrophobic character of several members of the group of cytolytic proteins termed ;thiol-activated'. Pneumolysin, alveolysin, cereolysin, and streptolysin O were found to be equally hydrophobic, as were the oxidized and reduced forms of alveolysin. Hydrophobic chromatography has been utilized in the development of an improved procedure for the purification of pneumolysin.
D001426:Bacterial Proteins; D002846:Chromatography, Affinity; D003603:Cytotoxins; D012685:Sepharose / Q000031:analogs & derivatives; D013301:Streptolysins / Q000302:isolation & purification; D013438:Sulfhydryl Compounds
D001426:Bacterial Proteins; D003603:Cytotoxins; D013301:Streptolysins; D013438:Sulfhydryl Compounds; C032290:plY protein, Streptococcus pneumoniae; C020927:phenyl-sepharose; D012685:Sepharose