Abstract
A simple and convenient method for the purification of the hemolytic toxin listeriolysin O (LLO) fromListeria monocytogenesis described. Supernatants from bacteria cultures were purified by application to a CH2spiral cartridge concentrator (Amicon) and ion exchange chromatography. A critical step is removal of contaminating RNA. The purified proteins had characteristics described for bacterial thiol-activated hemolysins: activation by a reducing agent (DTT) and inactivation by cholesterol. In addition, the molecular weight of 58,000 and pH-dependent hemolytic activity of this purified protein are consistent with the previously published characteristics of LLO.
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