Strong cation exchange-based fractionation of Lys-N-generated peptides facilitates the targeted analysis of post-translational modifications.

Journal article

In proteomics multi-dimensional fractionation techniques are widely used to reduce the complexity of peptide mixtures subjected to mass spectrometric analysis. Here, we describe the sequential use of strong cation exchange and reversed phase liquid chromatography in the separation of peptides generated by a relatively little explored metallo-endopeptidase with Lys-N cleavage specificity. When such proteolytic peptides are subjected to low-pH strong cation exchange we obtain fractionation prof...

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Authors: Taouatas, N; Altelaar, A; Drugan, M; Helbig, A; Mohammed, S

• Publication status: Published
• Journal: Molecular and cellular proteomics : MCP
• Volume: 8
• Issue: 1
• Pages: 190-200
• Publication date: 2009-01-01
• DOI: 10.1074/mcp.m800285-mcp200
• EISSN: 1535-9484
• ISSN: 1535-9476
• Language: English
• Keywords: Amino Acid Sequence; Cations; Chemical Fractionation; Humans; Peptides; Lysine; Mass Spectrometry; Acetylation; Protein Processing, Post-Translational; Molecular Sequence Data; Cell Line; Cell Extracts