Rocco J. Rotello and Timothy D. Veenstra* Pages 1 - 13 ( 13 )
In the current omics-age of research, major developments have been made in technologies that attempt to survey the entire repertoire of genes, transcripts, proteins, and metabolites present within a cell. While genomics has led to a dramatic increase in our understanding of such things as disease morphology and how organisms respond to medications, it is critical to obtain information at the proteome level since proteins carry out most of the functions within the cell. The primary tool for obtaining proteome-wide information on proteins within the cell is mass spectrometry (MS). While it has historically been associated with the protein identification, developments over the past couple of decades have made MS a robust technology for protein quantitation as well. Identifying quantitative changes in proteomes is complicated by its dynamic nature and the inability of any technique to guarantee complete coverage of every protein within a proteome sample. Fortunately, the combined development of sample preparation and MS methods have made it capable to quantitatively compare many thousands of proteins obtained from cells and organisms.
Quantitation, mass spectrometry, proteomics, isotope labeling, subtractive proteomics, SWATH-MS
School of Pharmacy, Cedarville University, Cedarville, OH 45314, School of Pharmacy, Cedarville University, Cedarville, OH 45314