Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2005-07-21

AUTHORS

W Andy Tao, Bernd Wollscheid, Robert O'Brien, Jimmy K Eng, Xiao-jun Li, Bernd Bodenmiller, Julian D Watts, Leroy Hood, Ruedi Aebersold

ABSTRACT

We present a robust and general method for the identification and relative quantification of phosphorylation sites in complex protein mixtures. It is based on a new chemical derivatization strategy using a dendrimer as a soluble polymer support and tandem mass spectrometry (MS/MS). In a single step, phosphorylated peptides are covalently conjugated to a dendrimer in a reaction catalyzed by carbodiimide and imidazole. Modified phosphopeptides are released from the dendrimer via acid hydrolysis and analyzed by MS/MS. When coupled with an initial antiphosphotyrosine protein immunoprecipitation step and stable-isotope labeling, in a single experiment, we identified all known tyrosine phosphorylation sites within the immunoreceptor tyrosine-based activation motifs (ITAM) of the T-cell receptor (TCR) CD3 chains, and previously unknown phosphorylation sites on total 97 tyrosine phosphoproteins and their interacting partners in human T cells. The dynamic changes in phosphorylation were quantified in these proteins. More... »

PAGES

591-598

Journal

TITLE

Nature Methods

ISSUE

8

VOLUME

2

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nmeth776

DOI

http://dx.doi.org/10.1038/nmeth776

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1017670964

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16094384


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