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PMID: 2512577 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Antibacterial peptides from pig intestine: isolation of a mammalian cecropin.

Lee JY, Boman A, Sun CX, Andersson M, Jörnvall H, Mutt V, Boman HG

Abstract

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.

MeSH Terms
Amino Acid Sequence Animals Anti-Bacterial Agents/isolation & purification,pharmacology Bacillus megaterium/drug effects Escherichia coli/drug effects Intestine, Small/analysis Microbial Sensitivity Tests Molecular Sequence Data Muscle, Smooth/analysis Peptides/isolation & purification,pharmacology Sequence Homology, Nucleic Acid Swine
Chemicals
Anti-Bacterial Agents Peptides
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Lee J Y
Department of Microbiology, University of Stockholm, Sweden.
Boman A
Sun C X
Andersson M
Jörnvall H
Mutt V
Boman H G
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17 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1989-12-00
Pages
9159-62
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC298453
Subset
IM
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