Simultaneous Identification of Tyrosine Phosphorylation and Sulfation Sites Utilizing Tyrosine-Specific Bromination
Autor: | Si-Uk Song, Hie-Joon Kim, Jong-Seo Kim |
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Rok vydání: | 2011 |
Předmět: |
Phosphopeptides
Halogenation Phosphatase Peptide Peptide Mapping Hydrobromic Acid chemistry.chemical_compound Sulfation Tandem Mass Spectrometry Structural Biology Catalytic Domain Tyrosine Phosphotyrosine Spectroscopy chemistry.chemical_classification Sulfatase Serum Albumin Bovine Tyrosine phosphorylation Peptide Fragments Phosphoric Monoester Hydrolases chemistry Biochemistry Acetylation Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Phosphorylation Sulfatases |
Zdroj: | Journal of the American Society for Mass Spectrometry. 22 |
ISSN: | 1044-0305 |
DOI: | 10.1007/s13361-011-0214-9 |
Popis: | Tyrosine phosphorylation and sulfation play many key roles in the cell. Isobaric phosphotyrosine and sulfotyrosine residues in peptides were determined by mass spectrometry using phosphatase or sulfatase to remove the phosphate or the sulfate group. Unique Br signature was introduced to the resulting tyrosine residues by incubation with 32% HBr at -20 °C for 20 min. MS/MS analysis of the brominated peptide enabled unambiguous determination of the phosphotyrosine and the sulfotyrosine sites. When phosphotyrosine and sulfotyrosine as well as free tyrosine were present in the same peptide, they could be determined simultaneously using either phosphatase or sulfatase following acetylation of the free tyrosine. |
Databáze: | OpenAIRE |
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