1c:{"metadata":[["$","title","0",{"children":"NIH VideoCast - Development of the Proteolytic 18O Labeling Method for Comparative Proteomics"}],["$","meta","1",{"name":"description","content":"As the sequencing is completed of many species' genomes, \nthe study of the protein compliment to the genome, or the proteome, has emerged as a dynamic field of research. A common approach to characterizing changed states is comparative proteomics, in which the relative amounts of proteins present in two or more samples are compared. In order to determine the \nrelative amount of the proteins present, a proteolytic method for 18O labeling can be used. Briefly, pools of proteins are enzymatically digested in parallel in H216O and H218O. In the latter pool two atoms of 18O are incorporated into the carboxyl-terminus of each new peptide. Comparative proteomic \nstudies can be performed by mixing the unlabeled peptide pool (generated in H216O) and the isotope labeled peptide pool (from H218O) and analyzing the peptide pairs by mass spectrometry. \n

\nMass Spectrometry Interest Group of the NCI at Frederick
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\nMass Spectrometry Interest Group of the NCI at Frederick
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\nMass Spectrometry Interest Group of the NCI at Frederick
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