De novo peptide sequencing and quantitative profiling of complex protein mixtures using mass-coded abundance tagging

peer-reviewed · Nature Biotechnology · 2002

peer-reviewed · Nature Biotechnology · 2002. Gerard Cagney et al. Proteomic studies require efficient, robust, and practical methods of characterizing proteins present in…
Date 2002-02-01
Type peer-reviewed
Venue Nature Biotechnology
Publisher Springer Science and Business Media LLC
Contribution adjacent
DOI 10.1038/nbt0202-163
Citations (OpenAlex) 231
Venue 2-year citedness 12.89

Abstract

Proteomic studies require efficient, robust, and practical methods of characterizing proteins present in biological samples. Here we describe an integrated strategy for systematic proteome analysis based on differential guanidination of C-terminal lysine residues on tryptic peptides followed by capillary liquid chromatography-electrospray tandem mass spectrometry. The approach, termed mass-coded abundance tagging (MCAT), facilitates the automated, large-scale, and comprehensive de novo determination of peptide sequence and relative quantitation of proteins in biological samples in a single analysis. MCAT offers marked advantages as compared with previously described methods and is simple, economic, and effective when applied to complex proteomic mixtures. MCAT is used to identify proteins, including polymorphic variants, from complex mixtures and measure variation in protein levels from diverse cell types.

Authors

  1. Gerard Cagney · University of Toronto
  2. Andrew Emili · University of Toronto

Methods and tools

  • MCAT: Mass-coded abundance tagging strategy for de novo peptide sequencing and quantitative profiling of complex protein mixtures.

Cites (4)

Cited by (14)

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