| Literature DB >> 22765043 |
Valentina Trinetta1, Anna Morleo, Fabio Sessa, Stefania Iametti, Francesco Bonomi, Pasquale Ferranti.
Abstract
Sakacin A was purified to homogeneity through simple chromatographic procedures from cultures of Lactobacillus sakei DSMZ 6333 grown on a low-cost medium. The highly purified protein dissipated both transmembrane potential (ΔΨ) and transmembrane pH gradient (ΔpH) in Listeria cells in a very intense, rapid, and energy-dependent fashion. On a slower timescale, purified sakacin A also showed a lytic activity toward isolated cell walls of Listeria. Mass spectrometry was used to analyze the products of sakacin A action on cell walls, evidencing that sakacin A acts on various types of bonds within peptoglycans.Entities:
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Year: 2012 PMID: 22765043 DOI: 10.1111/j.1574-6968.2012.02630.x
Source DB: PubMed Journal: FEMS Microbiol Lett ISSN: 0378-1097 Impact factor: 2.742