Journal article

+ 1 other files

Hydrophobic interaction chromatography for bottom-up proteomics analysis of single proteins and protein complexes

  • Rackiewicz, Michal Department of Biology, University of Fribourg, Switzerland - Department of Dermatology, Medical Center - University of Freiburg, Germany
  • Große-Hovest, Ludger SYNIMMUNE GmbH, Tübingen, Germany
  • Alpert, Andrew J. PolyLC Inc., Columbia, United States
  • Zarei, Mostafa Solvias AG, Kaiseraugst, Switzerland
  • Dengjel, Jörn Department of Biology, University of Fribourg, Switzerland - Department of Dermatology, Medical Center - University of Freiburg, Germany
Show more…
    02.06.2017
Published in:
  • Journal of Proteome Research. - 2017, vol. 16, no. 6, p. 2318–2323
English Hydrophobic interaction chromatography (HIC) is a robust standard analytical method to purify proteins while preserving their biological activity. It is widely used to study post-translational modifications of proteins and drug–protein interactions. In the current manuscript we employed HIC to separate proteins, followed by bottom-up LC–MS/MS experiments. We used this approach to fractionate antibody species followed by comprehensive peptide mapping as well as to study protein complexes in human cells. HIC–reversed-phase chromatography (RPC)–mass spectrometry (MS) is a powerful alternative to fractionate proteins for bottom-up proteomics experiments making use of their distinct hydrophobic properties.
Faculty
Faculté des sciences et de médecine
Department
Département de Biologie
Language
  • English
Classification
Biological sciences
License
License undefined
Identifiers
Persistent URL
https://folia.unifr.ch/unifr/documents/305515
Other files

Statistics

Document views: 30 File downloads:
  • den_hic.pdf: 56
  • den_hic_sm.pdf: 66