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Mapping Sites of Protein Phosphorylation by Mass Spectrometry Utilizing a Chemical-enzymatic Approach: Characterization of Products from Alpha-S1 Casein Phosphopeptides

Overview
Journal J Proteome Res
Specialty Biochemistry
Date 2005 Apr 13
PMID 15822919
Citations 1
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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 alpha-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.

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