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Zeitschriftenartikel

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

MPG-Autoren

Mirgorodskaya,  Ekaterina
Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50409

Lehrach,  Hans
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50168

Gobom,  Johan
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Volltexte (frei zugänglich)

Mirgorodskaya et al. - J Proteome Res.pdf
(beliebiger Volltext), 251KB

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Zitation

Mirgorodskaya, E., Wanker, E. E., Otto, A., Lehrach, H., & Gobom, J. (2005). Method for qualitative comparisons of protein mixtures based on enzyme-catalyzed stable-isotope incorporation. Journal of Proteome Research, 4(6), 2109-2116. doi:10.1021/pr050219i S1535-3893(05)00219-8.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-8581-5
Zusammenfassung
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.