Protein phosphorylation is directly or indirectly involved in all important cellular events. The understanding of its regulatory role requires the discovery of the proteins involved in these processes and how, where and when protein phosphorylation takes place. Investigation of the phosphoproteome of a cell is becoming feasible today although it still represents a very difficult task especially if quantitative comparisons have to be made. Several different experimental strategies can be employed to explore phosphoproteomes and this review will cover the most important ones such as incorporation of radiolabeled phosphate into proteins, application of specific antibodies against phosphorylated residues and direct staining of phosphorylated proteins in polyacrylamide gels. Moreover, methods to enrich phosphorylated proteins such as affinity chromatography (IMAC) and immunoprecipitation as well as mass spectrometry for identification of phosphorylated peptides and phosphorylation sites are also described.
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Review Article|
February 04 2005
Phosphoproteome Analysis
Roberto Raggiaschi;
Roberto Raggiaschi
1Sienabiotech S.p.A., Discovery Research, Via Fiorentina 1, 53100, Siena, Italy
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Stefano Gotta;
Stefano Gotta
1Sienabiotech S.p.A., Discovery Research, Via Fiorentina 1, 53100, Siena, Italy
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Georg C. Terstappen
Georg C. Terstappen
1Sienabiotech S.p.A., Discovery Research, Via Fiorentina 1, 53100, Siena, Italy
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Publisher: Portland Press Ltd
Online ISSN: 1573-4935
Print ISSN: 0144-8463
© 2005 Springer
2005
Biosci Rep (2005) 25 (1-2): 33–44.
Citation
Roberto Raggiaschi, Stefano Gotta, Georg C. Terstappen; Phosphoproteome Analysis. Biosci Rep 4 February 2005; 25 (1-2): 33–44. doi: https://doi.org/10.1007/s10540-005-2846-0
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