Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Anti-Bacterial Agents / pharmacology*
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Bacteriocins / chemistry
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Chromatography / methods
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Chromatography, High Pressure Liquid
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Electrophoresis, Polyacrylamide Gel
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Hemolymph / metabolism
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Hemolymph / microbiology
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Hydrogen-Ion Concentration
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Insect Proteins / chemistry
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Mass Spectrometry / methods
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Molecular Sequence Data
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Moths
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Peptides / chemistry
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Proline / chemistry
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Sequence Homology, Amino Acid
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Time Factors
Substances
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Anti-Bacterial Agents
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Bacteriocins
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Insect Proteins
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Peptides
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cecropin D protein, Hyalophora cecropia
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Proline