The hydrophobic character of thiol-activated cytolysins

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Abstract
Hydrophobic chromatography on phenyl-Sepharose revealed the decidedly hydrophobic character of several members of the group of [bacterial] cytolytic proteins termed thiol-activated. Pneumolysin, alveolysin, cereolysin and streptolysin O were equally hydrophobic, as were the oxidized and reduced forms of alveolysin. Hydrophobic chromatography was used in the development of an improved procedure for the purification of pneumolysin.

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