Prophenin-1, an exceptionally proline-rich antimicrobial peptide from porcine leukocytes

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...

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Bibliographic Details
Published in:FEBS letters 1995-03, Vol.362 (1), p.65-69
Main Authors: Harwig, Sylvia S.L, Kokryakov, Vladimir N, Swiderek, Kristine M, Aleshina, Galina M, Zhao, Chengquan, Lehrer, Robert I
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Anti-Bacterial Agents - chemistry
Anti-Bacterial Agents - isolation & purification
Anti-Bacterial Agents - pharmacology
Antimicrobial
Cathelin
Escherichia coli
Escherichia coli - drug effects
Leukocytes - chemistry
Listeria monocytogenes
Listeria monocytogenes - drug effects
Microbial Sensitivity Tests
Molecular Sequence Data
Molecular Weight
Peptide
Porcine leukocyte
Proline-rich
Proteins - chemistry
Proteins - isolation & purification
Proteins - pharmacology
Swine - blood
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(95)00210-Z