Development of a novel chemical probe for the selective enrichment of phosphorylated serine- and threonine-containing peptides

  • van der Veken, P.
  • Dirksen, E.H.C.
  • Ruijter, E.
  • Elgersma, R.C.
  • Heck, A.J.R.
  • Rijkers, D.T.S.
  • Slijper, M.
  • Liskamp, R.M.J.
Publication date
December 2005
Publisher
Wiley
ISSN
1439-4227
Citation count (estimate)
49

Abstract

Gaining insight into phosphoproteomes is of the utmost importance for understanding regulation processes such as signal transduction and cellular differentiation. While the identification of phosphotyrosine-containing amino acid sequences in peptides and proteins is now becoming possible, mainly because of the availability of high-affinity antibodies, no general and robust methodology allowing the selective enrichment and analysis of serine- and threonine-phosphorylated proteins and peptides is presently available. The method presented here involves chemical modification of phosphorylated serine or threonine residues and their subsequent derivatization with the aid of a multifunctional probe molecule. The designed probe contains four parts:...

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