Improved Detection of Hydrophilic Phosphopeptides Using Graphite Powder Microcolumns and Mass Spectrometry
نویسندگان
چکیده
منابع مشابه
Characterisation of phosvitin phosphopeptides using MALDI-TOF mass spectrometry.
Putative phosphopeptides produced from enzyme hydrolysis of phosvitin were identified and characterised using MALDI-TOF/MS. Phosvitin was heat-pretreated and then hydrolysed using pepsin, thermolysin, and trypsin at their optimal pH and temperature conditions with or without partial dephosphorylation. Pepsin and thermolysin were not effective in producing phosphopeptides, but trypsin hydrolysis...
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The reversible phosphorylation of proteins is a dynamic process that plays a major role in many vital physiological processes by transmitting signals within cellular pathways and networks. Proteomic measurements using mass spectrometry are capable of characterizing the sites of protein phosphorylation and to quantify their change in abundance. However, the low stoichiometry of protein phosphory...
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In recent years, forensic scientists have become increasingly interested in the detection and interpretation of organic gunshot residues (OGSR) due to the increasing use of lead- and heavy metal-free ammunition. This has also been prompted by the identification of gunshot residue- (GSR-) like particles in environmental and occupational samples. Various techniques have been investigated for thei...
متن کاملGlobal proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.
Electron transfer dissociation (ETD) is a recently introduced mass spectrometric technique that provides a more comprehensive coverage of peptide sequences and posttranslational modifications. Here, we evaluated the use of ETD for a global phosphoproteome analysis. In all, we identified a total of 1,435 phosphorylation sites from human embryonic kidney 293T cells, of which 1,141 ( approximately...
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Phosphorylation is a post-translational modification (PTM) fundamental for processes such as signal transduction and enzyme activity. We propose to apply data-independent acquisition (DIA) using mass spectrometry (MS) to determine unexplored phosphorylation events on isobarically modified peptides. Such peptides are commonly not quantitatively discriminated in phosphoproteomics due to their ide...
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ژورنال
عنوان ژورنال: Molecular & Cellular Proteomics
سال: 2004
ISSN: 1535-9476
DOI: 10.1074/mcp.m300105-mcp200