抄録
Mass spectrometry represents a well-accepted and reliable method for characterization of proteins. The method has great advantages in terms of high throughput, high accuracy, and high sensitivity in measurements, which is well suited for the identification of a wide variety of proteins, such those separated by 2D-PAGE, and for the analysis of post-transnational modifications, which play important roles in various biological events. Taking advantages of accumulating protein/DNA sequence databases, the former has been a routine task for overall profiling of proteins expressed in a cell or tissue. The latter, especially, the analysis of unknown or multiple modifications, is a challenging work and could be achieved by the cutting-edge MS techniques such as high-accuracy mass measurement and tandem MS. I here wish to describe the current status of MS in proteomics research and its capability for the structural analysis of various kinds of modifications such as lipidation, phosphorylation, glycosylation, etc.
