title: Isolation, purification and partial amino acid sequence of a highly hydrophobic new microcin named microcin L produced by Escherichia coli.
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.
authors.affiliation: Laboratoire de Génie Protéique et Cellulaire, Université de La Rochelle, France.
authors.forename: S
authors.initials: S
authors.lastname: Gaillard-Gendron
authors.forename: D
authors.initials: D
authors.lastname: Vignon
authors.forename: G
authors.initials: G
authors.lastname: Cottenceau
authors.forename: M
authors.initials: M
authors.lastname: Graber
authors.forename: N
authors.initials: N
authors.lastname: Zorn
authors.forename: A
authors.initials: A
authors.lastname: van Dorsselaer
authors.forename: A M
authors.initials: AM
authors.lastname: Pons
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001430:Bacteriocins / Q000737:chemistry* / Q000302:isolation & purification* / Q000494:pharmacology; D004926:Escherichia coli / Q000737:chemistry* / Q000187:drug effects / Q000378:metabolism; D006358:Hot Temperature; D013058:Mass Spectrometry; D008969:Molecular Sequence Data
chemical_list: D000596:Amino Acids; D001430:Bacteriocins; C020411:microcin