, Volume 213, Issue 4, pp 586–593

Matrix-assisted laser desorption/ionization time of flight mass spectrometry peptide mass fingerprints and post source decay: a tool for the identification and analysis of phloem proteins from Cucurbita maxima Duch. separated by two-dimensional polyacrylamide gel electrophoresis

Original Article

DOI: 10.1007/s004250100523

Cite this article as:
& Planta (2001) 213: 586. doi:10.1007/s004250100523


A combination of gel electrophoresis and mass spectrometry was used to analyze the soluble proteins from phloem sap of Cucurbita maxima Duch. Phloem proteins were separated using two-dimensional gel electrophoresis. Coomassie-stained spots were cut out and subjected to tryptic digestion. To identify proteins, peptide mass fingerprints were determined by matrix-assisted laser desorption/ionization time of flight (MALDI-TOF) mass spectrometry. In addition, MALDI-TOF post source decay measurements were used to obtain partial sequence information for the proteins. Results from both approaches were used for database searches. In this study, 17 proteins in the mass range 5–50 kDa were analyzed. Of these proteins six could be clearly identified, seven showed significant homologies to known plant proteins, and four were not significantly homologous to database entries. The present study suggests that the applied method is feasible for a large-scale analysis and identification of phloem proteins derived from different organs or from plants kept under various physiological conditions.

Cucurbita (phloem proteins) Phloem protein identification Protein (phloem) 

Copyright information

© Springer-Verlag 2001

Authors and Affiliations

    • 1
    • 2
  1. 1.Zentrum für Biopolymere, Universität Potsdam, Karl-Liebknecht-Strasse 24–25, Haus 20, 14476 Golm, Germany
  2. 2.Max-Planck-Institut für Molekulare Pflanzenphysiologie, Am Mühlenberg 1, 14476 Golm, Germany

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