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 p...

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Veröffentlicht in:	Acta biochimica polonica 2001-01, Vol.48 (4), p.1191-1195
Hauptverfasser:	Mak, P, Chmiel, D, Gacek, G J
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Anti-Bacterial Agents - pharmacology Bacteriocins - chemistry Chromatography - methods Chromatography, High Pressure Liquid Electrophoresis, Polyacrylamide Gel Hemolymph - metabolism Hemolymph - microbiology Hydrogen-Ion Concentration Insect Proteins - chemistry Mass Spectrometry - methods Molecular Sequence Data Moths Peptides - chemistry Proline - chemistry Sequence Homology, Amino Acid Time Factors
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Beschreibung
Zusammenfassung:	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.
ISSN:	0001-527X 1734-154X
DOI:	10.18388/abp.2001_3890