Development of Proteomic Tools for Monitoring Peptide and Protein Phosphorylation

Development of Proteomic Tools for Monitoring Peptide and Protein Phosphorylation

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Protein phosphorylation is considered a key posttranslational modification regulating many cellular functions, including signal transduction, gene expression, protein synthesis, muscle contraction, and cell metabolism. Development of novel phosphoproteins and phosphopeptides analysis methods is essential for understanding various disease states and cellular processes associated with phosphorylation. Oxidation reduction condensation was used to modify phosphopeptide and phosphoproteins towards analyzing protein and peptide phosphorylation. Initially the reactivity of phosphate and other functional groups towards oxidation reduction condensation was assessed with synthetic phosphopeptides and unphosphorylated peptides. The oxidation-reduction condition was optimized as a two-step method to modify phosphoserine, phosphothreonine and phosphotyrosine phosphorylation. The two-step method was used to enrich phosphoserine, phosphothreonine, and phosphotyrosine peptides from synthetic peptide mixture using solid phase capture. Dansyl amine and biotin amine were attached on phosphopeptides using the oxidation reduction condensation, indicating its compatibility with various functional moieties. Phosphorylated beta-casein was visualized with dansyl modification after gel electrophoresis. In addition, biotin attachment was used as a solution phase enrichment method. The strategy based on direct chemical modification of phosphate group is promising as a chemical tool for analyzing protein phosphorylation.... charged phosphate group and the metal chelating matrix.........................24 Figure 1.19 Phosphoprotein enrichment from immobilized metal affinity chromatography (IMAC)...................................................24 Figure 1.20 I²-elimination of phosphateanbsp;...

Title:Development of Proteomic Tools for Monitoring Peptide and Protein Phosphorylation
Author: Agnes Mangalika W. V. Arachchige Dona
Publisher:ProQuest - 2007

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