Localization of In Vivo Phosphorylation Sites in Multiphosphorylated Proteins

Application of S-Ethylcysteine Derivatization and Mass Spectrometric Analysis
  • Esben S. Sørensen
  • Lone K. Rasmussen
  • Peter Højrup
  • Torben E. Petersen


Phosphorylation of proteins is one of the most frequent forms of posttranslational modification in eukaryotic cells and is linked to the control of a multitude of cellular functions. Proteins involved in this type of regulation are typically only phosphorylated at a single or a few sites. Another type of phosphoproteins are those containing multiple phosphorylations. In these proteins the phosphorylations usually possess different functions than in proteins phosphorylated at single sites. In the case of multisite phosphorylated proteins (for review see Roach, 1991), the phosphorylations are often important as physical interactors with divalent metal ions, especially Cat2+.


Phosphorylation Site Amino Acid Analysis Mass Spectrometric Analysis Bovine Milk Potential Phosphorylation Site 
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Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • Esben S. Sørensen
    • 1
  • Lone K. Rasmussen
    • 1
  • Peter Højrup
    • 2
  • Torben E. Petersen
    • 1
  1. 1.Protein Chemistry LaboratoryUniversity of AarhusAarhus CDenmark
  2. 2.Department of Molecular BiologyUniversity of OdenseOdense MDenmark

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