Plasma desorption mass spectrometry coupled with conventional peptide sequencing techniques.
The mass of intact and enzymatically derived fragments of cecropin B, an antibacterial protein from the Chinese oak silk moth, Antherea pernyi, have been determined by 252Cf plasma desorption time-of-flight mass spectrometry. As a result, the carboxy terminal amino acid sequence of the protein was established.
D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents; D007301:Insect Hormones / Q000032:analysis; D019476:Insect Proteins; D013058:Mass Spectrometry / Q000379:methods*; D008969:Molecular Sequence Data; D009036:Moths; D012697:Serine Endopeptidases
D000900:Anti-Bacterial Agents; D007301:Insect Hormones; D019476:Insect Proteins; C031162:cecropin B protein, Insecta; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase