Isolation, purification and partial amino acid sequence of a highly hydrophobic new microcin named microcin L produced by Escherichia coli.
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.
Gaillard-Gendron
S
S
Laboratoire de Génie Protéique et Cellulaire, Université de La Rochelle, France.
Vignon
D
D
Cottenceau
G
G
Graber
M
M
Zorn
N
N
van Dorsselaer
A
A
Pons
A M
AM
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
D000596:Amino Acids; D001430:Bacteriocins; C020411:microcin