Antibacterial peptides of the moth Galleria mellonella.
The work describes purification and biochemical characterization of two inducible antimicrobial peptides from the hemolymph of Galleria mellonella. The peptides were isolated by a sequence of reversed-phase chromatography steps from the hemolymph of larvae immunized with viable bacteria. The first peptide is a member of the cecropin family while the second one is rich in proline residues and has a unique sequence.
Mak
P
P
Institute of Molecular Biology, Jagiellonian University, Kraków, Poland. makp@mol.uj.edu.pl
Chmiel
D
D
Gacek
G J
GJ
D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001430:Bacteriocins / Q000737:chemistry; D002845:Chromatography / Q000379:methods; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006458:Hemolymph / Q000378:metabolism / Q000382:microbiology; D006863:Hydrogen-Ion Concentration; D019476:Insect Proteins / Q000737:chemistry; D013058:Mass Spectrometry / Q000379:methods; D008969:Molecular Sequence Data; D009036:Moths; D010455:Peptides / Q000737:chemistry; D011392:Proline / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D013997:Time Factors
D000900:Anti-Bacterial Agents; D001430:Bacteriocins; D019476:Insect Proteins; D010455:Peptides; C036149:cecropin D protein, Hyalophora cecropia; D011392:Proline