Proteomics Approach to Identifying ATP-Covalently Modified Proteins

Paul Besant, M.V. Lasker, C.G. Bui, E. Tan, Paul Attwood, C.W. Turck

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


This study aims to investigate functionally similar proteins based on their capacity to remain bound to ATP under stringent resolving conditions. Using two-dimensional gel electrophoresis and capillary liquid chromatography on-line mass spectrometry, we have identified several mammalian and E. coli proteins that appear to covalently bind ATP. To validate this approach, we obtained commercially purified forms of proteins identified from two-dimensional protein maps and tested their capacity to bind alpha P-32 phosphate labeled ATP. This proteomics approach provides an initial screening method of identifying functionally similar proteins for further scrutiny by a more traditional analysis.
Original languageEnglish
Pages (from-to)120-125
JournalJournal of Proteome Research
Issue number1
Publication statusPublished - 2004


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