Simultaneous analysis of phosphorylated peptides by MALDI-TOF-MS

J. H. Kang, R. Toita, Y. Jiang, T. Niidome, Y. Katayama

    Research output: Contribution to journalArticlepeer-review

    10 Citations (Scopus)

    Abstract

    Six peptides with various phosphorylation sensitivities for protein kinase A (PKA) were used for the simultaneous analysis of phosphorylated peptides using matrix-assisted laser desorption/ionization-time-of-flight (MALDI-TOF) mass spectrometry. The mixture of six peptides was reacted with PKA and was analyzed by MALDI-TOF mass spectrometry. The intensity of all peaks except one phosphorylated peptide peak was very low (<20%). Moreover, we examined whether the addition of diammonium citrate to CHCA matrix at concentrations of 1-20 mg mL-1 can increase the peak intensity of peptides and phosphorylated peptides. The addition of diammonium citrate increased the peak intensity of peptides and phosphorylated peptides, but an increase in the intensity was unsatisfactory. Our study strongly suggests that MALDI-TOF mass spectrometry is not suitable for the simultaneous analysis of phosphorylated peptides.

    Original languageEnglish
    Pages (from-to)595-598
    Number of pages4
    JournalChromatographia
    Volume63
    Issue number11-12
    DOIs
    Publication statusPublished - Jun 2006

    All Science Journal Classification (ASJC) codes

    • Analytical Chemistry
    • Biochemistry
    • Clinical Biochemistry
    • Organic Chemistry

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