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pubmed-article:15822919pubmed:abstractTextA 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.lld:pubmed
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pubmed-article:15822919pubmed:authorpubmed-author:McCormickDani...lld:pubmed
pubmed-article:15822919pubmed:authorpubmed-author:MuddimanDavid...lld:pubmed
pubmed-article:15822919pubmed:authorpubmed-author:HolmesMichael...lld:pubmed
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pubmed-article:15822919pubmed:dateRevised2009-11-18lld:pubmed
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pubmed-article:15822919pubmed:articleTitleMapping sites of protein phosphorylation by mass spectrometry utilizing a chemical-enzymatic approach: characterization of products from alpha-S1 casein phosphopeptides.lld:pubmed
pubmed-article:15822919pubmed:affiliationDepartment of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Mayo Clinic, Rochester, Minnesota 55905, USA. mccormick.daniel@mayo.edulld:pubmed
pubmed-article:15822919pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15822919pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed