Mapping sites of protein phosphorylation by mass spectrometry utilizing a chemical-enzymatic approach: Characterization of products from α-S1casein phosphopeptides

Daniel J. McCormick, Michael W. Holmes, David C. Muddiman, Benjamin J. Madden

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

A novel chemical-enzymatic approach was developed to facilitate identification of phosphorylation sites in isolated phosphoproteins. ESI-TOF mass spectrometry was used to characterize products from the chemical-enzymatic cleavage of specific phosphorylation sites in bovine α-S1 casein and synthetic phosphopeptides containing substitutions at a single phosphorylation site. Further refinements to this approach for identification of protein phosphorylation sites and its utility for the quantification of phosphopeptides by isotope-dilution mass spectrometry are presented.

Original languageEnglish (US)
Pages (from-to)424-434
Number of pages11
JournalJournal of Proteome Research
Volume4
Issue number2
DOIs
StatePublished - Mar 1 2005

Keywords

  • 2-Aminoethanethiol
  • Chemical-enzymatic
  • Isotope dilution mass spectrometry
  • Phosphopeptides
  • Phosphoproteins
  • Phosphorylation
  • Quantification

ASJC Scopus subject areas

  • Biochemistry
  • Chemistry(all)

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