Analysis of Protein Phosphorylation by Mass Spectrometry
| Autor: | Vittoria Matafora, Angela Bachi, Liliana B. Areces |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
Chemistry
010401 analytical chemistry General Medicine Phosphoproteins 010402 general chemistry Mass spectrometry Proteomics 01 natural sciences Mass Spectrometry Atomic and Molecular Physics and Optics 0104 chemical sciences Biochemistry Phosphoprotein Stable isotope labeling by amino acids in cell culture Phosphorylation Protein phosphorylation Tyrosine Threonine Spectroscopy |
| Zdroj: | European Journal of Mass Spectrometry. 10:383-392 |
| ISSN: | 1751-6838 1469-0667 |
| DOI: | 10.1255/ejms.601 |
| Popis: | Phosphorylation is one of the most frequently occurring post-translational modifications in proteins. In eukaryotic cells, protein phosphorylation on serine, threonine and tyrosine residues plays a crucial role as a modulator of protein function. A comprehensive analysis of protein phosphorylation involves the identification of the phosphoproteins, the exact localization of the residues that are phosphorylated and the quantitation of phosphorylation. In this short review we will summarize and discuss the methodologies currently available for the analysis and full characterization of phosphoproteins with emphasis on mass spectrometry-based techniques. In particular, we will discuss affinity-based purification of phosphopeptides coupled to matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI ToF-MS) analysis, their detection using mass mapping and precursor-ion scans, identification of modified sites by tandem mass spectrometry (MS/MS) and quantitative analysis. |
| Databáze: | OpenAIRE |
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