Simultaneous analysis of phosphorylated peptides by MALDI-TOF-MS

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

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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 1 2006

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry
  • Biochemistry
  • Clinical Biochemistry
  • Organic Chemistry

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