Partial 18 O-labeling of peptides has been applied to post-source decay experiments in a matrix-assisted laser desorption/ionization time-of-flight mass spectrometer. The ions which originate from the carboxyl terminus of a peptide partially retain 18 O atoms which have readily been incorporated int
A strategy for rapid and efficient sequencing of Lys-C peptides by matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry post-source decay
✍ Scribed by Thomas Pfeifer; Peter Rücknagel; Gerhard Kuellertz; Angelika Schierhorn
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 102 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0951-4198
No coin nor oath required. For personal study only.
✦ Synopsis
A modification procedure for Lys-C peptides is described which simplifies the correct assignment of the amino acid sequence. Release of the C-terminal lysine from Lys-C peptides by carboxypeptidase B and subsequent N-terminal acetylation of the resulting peptides leads to predictable shifts of the C-and Nterminal fragment ions in Matrix-assisted laser desorption/ionisation time-of-flight post-source decay mass spectra and facilitates the correct assignment of mostly complete amino acid sequences for oligopeptides. The derived sequences of peptides from unknown proteins were used to search in databases for homologous protein sequences. Our method was applied to an unknown protein isolated from eggs of Drosophila melanogaster, resulting in the identification of a peptidyl prolyl cis-trans-isomerase.
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