Targeting phosphoprotein profiling by combination of hydroxyapatite-based phosphoprotein enrichment and SELDI-TOF MS

Arch Physiol Biochem. 2010 Oct-Dec;116(4-5):181-7. doi: 10.3109/13813455.2010.506219. Epub 2010 Aug 23.

Abstract

Over the last decade surface-enhanced laser desorption/ionization time-of-flight mass spectrometry (SELDI-TOF MS) has evolved as a versatile tool in the field of proteomic research. Although the chromatographic matrices on the currently provided SELDI affinity arrays allow efficient on-chip protein enrichment, it can be advantageous to combine SELDI with additional sample pre-fractionation steps. In this study, we demonstrate the potential of combining hydroxyapatite-based phosphoprotein enrichment with SELDI-TOF MS analysis. A straightforward method for the enrichment of phosphoproteins on ceramic hydroxyapatite was developed using fluorescently-labelled model proteins. Hydroxyapatite-based pre-fractionation of proteins derived from cell lysates was performed. SELDI-TOF MS analysis of the pre-fractionation eluate confirmed a considerable reduction of sample complexity and an enhancement of selected protein signals.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cells, Cultured
  • Chemical Fractionation / methods*
  • Chromatography, Affinity* / methods
  • Durapatite* / chemistry
  • Electrophoresis, Polyacrylamide Gel
  • Embryonic Stem Cells / chemistry
  • Fluorescent Dyes
  • Fluorometry
  • Mice
  • Phosphoproteins* / analysis
  • Phosphoproteins* / chemistry
  • Phosphorylation
  • Protein Array Analysis / methods*
  • Protein Isoforms / analysis*
  • Protein Isoforms / chemistry*
  • Proteins / analysis*
  • Proteins / chemistry*
  • Proteome* / analysis
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization* / methods

Substances

  • Fluorescent Dyes
  • Phosphoproteins
  • Protein Isoforms
  • Proteins
  • Proteome
  • Durapatite