1. A method for purification of listeriolysin O from a hypersecretor strain of Listeria monocytogenes.
- Author
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Walton CM, Wu CH, and Wu GY
- Subjects
- Cholesterol pharmacology, Chromatography, Ion Exchange, Culture Media, Conditioned chemistry, Dithiothreitol pharmacology, Heat-Shock Proteins antagonists & inhibitors, Heat-Shock Proteins biosynthesis, Hemolysin Proteins, Hemolysis drug effects, Bacterial Toxins, Heat-Shock Proteins isolation & purification, Listeria monocytogenes metabolism
- Abstract
A simple and convenient method for the purification of the hemolytic toxin listeriolysin O (LLO) from Listeria monocytogenes is described. Supernatants from bacteria cultures were purified by application to a CH2 spiral 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., (Copyright 1999 Academic Press.)
- Published
- 1999
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