Abstract
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.
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Selected References
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