Mapping sites of protein phosphorylation by mass spectrometry utilizing a chemical-enzymatic approach

Characterization of products from α-S1casein phosphopeptides

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

Research output: Contribution to journalArticle

7 Citations (Scopus)

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 2005

Fingerprint

Phosphopeptides
Phosphorylation
Mass spectrometry
Mass Spectrometry
Proteins
Electrospray Ionization Mass Spectrometry
Phosphoproteins
Caseins
Isotopes
Dilution
Substitution reactions

Keywords

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

ASJC Scopus subject areas

  • Genetics
  • Biotechnology
  • Biochemistry

Cite this

Mapping sites of protein phosphorylation by mass spectrometry utilizing a chemical-enzymatic approach : Characterization of products from α-S1casein phosphopeptides. / Mc Cormick, Daniel J; Holmes, Michael W.; Muddiman, David C.; Madden, Benjamin J.

In: Journal of Proteome Research, Vol. 4, No. 2, 03.2005, p. 424-434.

Research output: Contribution to journalArticle

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