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- W2035820170 abstract "We report here the production, by an Escherichia coli strain, of two microcins, microcin J25 and a new one that we designated microcin L. The active peptides were separated by solid phase extraction on C(18) cartridges. Microcin L was then purified to homogeneity by cationic-exchange high-performance liquid chromatography. Its molecular mass, determined by mass spectrometry, is 8899 Da. The amino acid composition and the sequence of the first 40 N-terminal residues indicate that microcin L is a hydrophobic peptide, which exhibits high homology to gassericin and lactacin F which both belong to the class II bacteriocins." @default.
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- W2035820170 date "2000-12-01" @default.
- W2035820170 modified "2023-09-27" @default.
- W2035820170 title "Isolation, purification and partial amino acid sequence of a highly hydrophobic new microcin named microcin L produced by<i>Escherichia coli</i>" @default.
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- W2035820170 doi "https://doi.org/10.1111/j.1574-6968.2000.tb09408.x" @default.
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