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Linking protein fractionation with multidimensional monolithic reversed-phase peptide chromatography/mass spectrometry enhances protein identification from complex mixtures even in the presence of abundant proteins

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons97478

Wienkoop,  S.
Integrative Proteomics and Metabolomics, Department Stitt, Max Planck Institute of Molecular Plant Physiology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons97171

Glinski,  M.
Integrative Proteomics and Metabolomics, Department Stitt, Max Planck Institute of Molecular Plant Physiology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons97446

Tolstikov,  V.
Metabolomic Analysis, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons97148

Fiehn,  O.
Metabolomic Analysis, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons97471

Weckwerth,  W.
Integrative Proteomics and Metabolomics, Department Stitt, Max Planck Institute of Molecular Plant Physiology, Max Planck Society;

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Citation

Wienkoop, S., Glinski, M., Tanaka, N., Tolstikov, V., Fiehn, O., & Weckwerth, W. (2004). Linking protein fractionation with multidimensional monolithic reversed-phase peptide chromatography/mass spectrometry enhances protein identification from complex mixtures even in the presence of abundant proteins. Rapid Communications in Mass Spectrometry, 18(6), 643-650. doi:10.1002/rcm.1376.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0014-2C3C-7
Abstract