In situ N‐phosphorylation of oligopeptides for fast atom bombardment mass spectrometry
- 1 June 1992
- journal article
- account
- Published by Wiley in Journal of Mass Spectrometry
- Vol. 27 (6), 746-749
- https://doi.org/10.1002/oms.1210270618
Abstract
Positive ion fast atom bombardment mass spectrometry (FABMS) of in situ N‐phosphorylated oligopeptides showed intense quasi‐molecular ions together with the successive alkene loss fragment ions, which afford multiple checks of the unequivocal reality of the relative molecular mass of the tested samples. More interesting, in a novel cleavage pattern only the N‐phosphoryl fragment ions gave intense peaks, the C‐terminal series ions being suppressed. For each of the N‐terminal ions, losses of alkenes also occur to provide multiple checks for the existence of these ions. The FABMS of the in situ N‐ phosphorylated oligopeptides might provide an easily accessible routine method for peptide sequencing.This publication has 6 references indexed in Scilit:
- Fragmentation characteristics ofN-dialkyloxyphosphinylpeptides under fast atom bombardmentJournal of Mass Spectrometry, 1991
- A novel reagent, dialkylphosphite, for peptide synthesisInternational Journal of Peptide and Protein Research, 1991
- Novel fragmentation ofN-diisopropyloxyphosphoryl dipeptides and tripeptides by fast atom bombardment mass spectrometryJournal of Mass Spectrometry, 1991
- N-phosphoryl amino acids and peptides. Part II: Fast atom bombardment mass spectrometry ofN-di-isopropyloxyphosphoryl andN-dibutyloxyphosphoryl amino acidsJournal of Mass Spectrometry, 1989
- Improvement in sensitivity of fast atom bombardment mass spectrometry of amino acids by di-isopropylphosphorylationJournal of Mass Spectrometry, 1987
- Mass spectrometric determination of the amino acid sequence of peptides and proteinsMass Spectrometry Reviews, 1987