Functional proteomics, quantitative mass

Quantitative Mass Spectrometry for Comparative and Functional Proteomics... 

Wei, Y., and Chen, S.S. (2005) Mass spectrometry-based quantitative proteomic profiling. Briefings in functional genomics and proteomics 4, 1-12. 

Mass spectrometry has been applied mainly in proteome research, but also in discovery and quantitation of neuropeptides that are involved in pain mechanisms, such as nocistatin, substance P, or verification of, for example, the structure of endogenous morphine in the central nervous system. Some proteomics studies of pain are aimed at the search for pain markers in cerebrospinal fluid, as it may reflect changes in brain and spinal cord functioning. Another research area concerns proteome analysis in cancer pain using spinal cord tissue and animal models. 

The above methods have opened a new door to tackle quantitative proteomics by element mass spectrometry, although it is still quite difficult to quantify proteins by element mass spectrometry detection after element labeling. In fact, element labeling is not a new concept. For example, a silver saturation assay was applied for measurement of metallothionein in tissue. But this kind of metal-binding assay is based on certain properties of a protein and, being less selective, is applied mainly for a known and isolated protein. Comparatively, bi-functional chelating reagents are established in selective, reproducible reactions and thus are more suitable for protein quantification by element mass spectrometry detection. 

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