期刊
JOURNAL OF PROTEOME RESEARCH
卷 1, 期 1, 页码 47-54出版社
AMER CHEMICAL SOC
DOI: 10.1021/pr015509n
关键词
gene expression; functional genomics; proteomics; protein profiling; mass spectrometry; isotope-coded affinity tags
资金
- NATIONAL CANCER INSTITUTE [R33CA084698] Funding Source: NIH RePORTER
- NCI NIH HHS [1R33CA84698] Funding Source: Medline
- NHGRI NIH HHS [HG00041] Funding Source: Medline
The effectiveness of proteome-wide protein identification and quantitative expression profiling is dependent on the ability of the analytical methodologies employed to routinely obtain information on low-abundance proteins, as these are frequently of great biological importance. Two-dimensional gel electrophoresis, the traditional method for proteome analysis, has proven to be biased toward highly expressed proteins. Recently, two-dimensional chromatography of the complex peptide mixtures generated by the digestion of unseparated protein samples has been introduced for the identification of their components, and isotope-coded affinity tags (ICAT) have been introduced to allow for accurate quantification of the components of protein mixtures by mass spectrometry. Here, we demonstrate that the combination of isotope coded affinity protein tags and multidimensional chromatography/mass spectrometry of tryptic peptide mixtures is capable of detecting and quantifying proteins of low abundance in complex samples.
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