Abstract
We purified and characterized an unusual antimicrobial peptide, prophenin-1 (PF-1), from porcine leukocytes. The peptide had a mass of 8,683 and contained 79 residues, including 42 (53.2%) prolines and 15 (19.0%) phenylalanines. Its N-terminal 60 residues consisted of three perfect and three nearly perfect repeats of a decamer, FPPPNFPGPR. Prophenin-1 was encoded on a cathelin-containing precursor and showed substantially more activity against E. coli, a Gram-negative bacterium, than against Listeria monocytogenes, a Gram-positive organism, in vitro.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Anti-Bacterial Agents / chemistry*
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Anti-Bacterial Agents / isolation & purification
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Anti-Bacterial Agents / pharmacology*
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Antimicrobial Cationic Peptides
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Escherichia coli / drug effects
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Leukocytes / chemistry*
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Listeria monocytogenes / drug effects
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Microbial Sensitivity Tests
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Molecular Sequence Data
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Molecular Weight
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Proteins / chemistry*
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Proteins / isolation & purification
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Proteins / pharmacology*
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Swine / blood
Substances
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Anti-Bacterial Agents
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Antimicrobial Cationic Peptides
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Proteins
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prophenin 1