Mapping Sites of Protein Phosphorylation by Mass Spectrometry Utilizing a Chemical-enzymatic Approach: Characterization of Products from Alpha-S1 Casein Phosphopeptides
Overview
Affiliations
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.
Wang L, Harshman S, Liu S, Ren C, Xu H, Sallans L Proteomics. 2010; 10(23):4281-92.
PMID: 21110323 PMC: 3021470. DOI: 10.1002/pmic.201000080.