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Method for qualitative comparisons of protein mixtures based on enzyme-catalyzed stable-isotope incorporation

Item Type:Article
Title:Method for qualitative comparisons of protein mixtures based on enzyme-catalyzed stable-isotope incorporation
Creators Name:Mirgorodskaya, E., Wanker, E.E., Otto, A., Lehrach, H. and Gobom, J.
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 18O 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.
Keywords:18 o Labeling, Comparative Proteomics, MALDI, Mass Spectrometry, Nano-Liquid Chromatography, Protein Interactions, Stable Isotope
Source:Journal of Proteome Research
ISSN:1535-3893
Publisher:American Chemical Society
Volume:4
Number:6
Page Range:2109-2116
Date:1 November 2005
Official Publication:https://doi.org/10.1021/pr050219i
PubMed:View item in PubMed

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