Proteomics, mass spectrometry characterization techniques

Global proteomic techniques are used for biological problems for which no molecular entry point is known. The idea is that changes in a cellular system can be understood better by analyzing its entire protein content quantitatively. The main analytical tools are a global and quantitative protein display and mass spectrometry to characterize the proteins that were identified for showing relevant quantitative changes. 

Revisit the need for rat serum as the culmre medium. Characterize rat serum using modern proteomic techniques (e.g., MALDT mass spectrometry) to identify serum factors essential to normal in vitro embryonic growth and development. 

Recent developments in instrument design have led to lower limits of detection, while new ion activation techniques and improved understanding of gas-phase ion chemistry have enhanced the capabilities of tandem mass spectrometry for peptide and protein structure elucidation. Future developments must address the understanding of protein-protein interactions and the characterization of the dynamic proteome (Chalmers and Gaskell 2000). 

The first two protocols presented in this work focus on high-throughput gel-based techniques. Chapter 1 describes 2-D DICE, a method used to examine the entire proteome within discreet pi fractions, whereas Chapter 2 details several complementary techniques for the specific analysis of glycoproteins found in tissue samples. The next chapters. Chapters 3 and 4, focus on SELDI-MS and MALDI-TOF, two techniques that make use of mass spectrometry for the characterization and identification of proteins. These techniques may be used alone or in combination with other proteomic methods, such gel-based assays, where mass spectrometry is useful for additional characterization and identification of proteins. 

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