Antibacterial peptides from pig intestine: isolation of a mammalian cecropin.
Pig small intestine was used as starting material for a batchwise isolation of a peptide fraction enriched in antibacterial activities against Escherichia coli (anti-Ec factor) and against Bacillus megaterium (anti-Bm factor). Separation and further purification were by different types of chromatography. Sequence analysis showed the anti-Bm factor to be apparently similar to vasoactive intestinal peptide. The anti-Ec factor was found to have a 31-residue sequence that was cecropin-like. It was named cecropin P1 and its structure was confirmed by solid-phase synthesis. Synthetic cecropin P1 with and without C-terminal amide was assayed on eight different bacteria. Mobility comparison between synthetic and natural cecropin P1 indicates that the natural peptide has a free C-terminal carboxyl group.
Lee
J Y
JY
Department of Microbiology, University of Stockholm, Sweden.
Boman
A
A
Sun
C X
CX
Andersson
M
M
Jörnvall
H
H
Mutt
V
V
Boman
H G
HG
D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000302:isolation & purification* / Q000494:pharmacology; D001410:Bacillus megaterium / Q000187:drug effects; D004926:Escherichia coli / Q000187:drug effects; D007421:Intestine, Small / Q000032:analysis*; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D009130:Muscle, Smooth / Q000032:analysis; D010455:Peptides / Q000302:isolation & purification* / Q000494:pharmacology; D012689:Sequence Homology, Nucleic Acid; D013552:Swine
D000900:Anti-Bacterial Agents; D010455:Peptides