Identification of Protein Phosphorylation Sites by Mass Spectrometry
Part of the Springer Protocols Handbooks book series (SPH)
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In this chapter, methods will be reviewed for the identification of the type of modified amino acid residue (serine, threonine, or tyrosine) and position in the sequence of a phospho-protein/peptide.
KeywordsBinding Solution Calf Intestinal Alkaline Phosphatase Gallium Nitrate Aqueous Ammonium Hydroxide Modify Amino Acid Residue
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
- 6.Bartlet-Jones, M., Jeffery, W. A., Hansen, H. F., and Pappin, D. J. (1994) Peptide ladder sequencing by mass spectrometry using a novel, volatile degradation reagent. Rapid Comm. Mass Spec. 8, 737–742.Google Scholar
- 7.Larsen, M. R., Sorensen, G. L., Fey, S. J., Larsen, P. M., and Roepstorff, P. (2001) Phospho-proteomics: evaluation of the use of enzymatic de-phosphorylation and differential mass spectrometric peptide mass mapping for site specific phosphorylation assignment in pro-teins separated by gel electrophoresis. Proteomics 1, 223–238.PubMedCrossRefGoogle Scholar
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