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Simultaneous Analysis of Phosphorylated Peptides by MALDI-TOF-MS

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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.

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Authors and Affiliations

  1. Department of Applied Chemistry, Faculty of Engineering, Kyushu University, 744 Motooka, Nishi-Ku, Fukuoka, 819-0395, Japan

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

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  1. J. -H. Kang
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  2. R. Toita
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  3. Y. Jiang
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  4. T. Niidome
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  5. Y. Katayama
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Correspondence to Y. Katayama.

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Kang, J.H., Toita, R., Jiang, Y. et al. Simultaneous Analysis of Phosphorylated Peptides by MALDI-TOF-MS. Chroma 63, 595–598 (2006). https://doi.org/10.1365/s10337-006-0810-1

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  • DOI: https://doi.org/10.1365/s10337-006-0810-1

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