| Literature DB >> 10049682 |
C M Walton1, C H Wu, G Y Wu.
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.Entities:
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Year: 1999 PMID： 10049682 DOI： 10.1006/prep.1998.1022
Source DB: PubMed Journal: Protein Expr Purif ISSN： 1046-5928 Impact factor: 1.650