Method for qualitative comparisons of protein mixtures based on enzyme-catalyzed stable-isotope incorporation |
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Authors: | Mirgorodskaya Ekaterina Wanker Erich Otto Albrecht Lehrach Hans Gobom Johan |
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Affiliation: | Max Planck Institute for Molecular Genetics, Berlin, Germany. |
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Abstract: | Determining which proteins are unique among one or several protein populations is an often-encountered task in proteomics. To this purpose, we present a new method based on trypsin-catalyzed incorporation of the stabile isotope (18)O in the C-termini of tryptic peptides, followed by LC-MALDI MS analysis. The analytical strategy was designed such that proteins unique to a given population out of several can be assigned in a single experiment by the isotopic signal intensity distributions of their tryptic peptides in the recorded mass spectra. The method is demonstrated for protein-protein interaction analysis, in which the differential isotope labeling was used to distinguish endogenous human brain proteins interacting with a recombinant bait protein from nonbiospecific background binders. |
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