Improved matrix-assisted laser desorption/ionization mass spectrometric analysis of tryptic hydrolysates of proteins following guanidination of lysine-containing peptides

Francesco L. Brancia, Stephen G. Oliver, Simon J. Gaskell

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Analysis of tryptic digests of proteins using matrix-assisted laser desorption/ionization (MALDI) mass spectrometry commonly results in superior detection of arginine-containing peptides compared with lysine-containing counterparts. The effect is attributable in part to the greater stability of the arginine-containing peptide ions associated with the sequestration of the single ionizing proton on the arginine side-chain. Reaction of peptides with O-methylisourea resulted in conversion of lysine to homoarginine residues with consequent improved detection during MALDI-MS. Analysis of the underivatized tryptic digest of the yeast protein, enolase, revealed peptides representing 20% of the protein; the corresponding figure after derivatization was 46%. Copyright (C) 2000 John Wiley and Sons, Ltd.
    Original languageEnglish
    Pages (from-to)2070-2073
    Number of pages3
    JournalRapid communications in mass spectrometry : RCM
    Volume14
    Issue number21
    DOIs
    Publication statusPublished - 2000

    Research Beacons, Institutes and Platforms

    • Manchester Institute of Biotechnology

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