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Related Experiment Videos

Combining protein identification and quantification: C-terminal isotope-coded tagging using sulfanilic acid.

Alexandre Panchaud1, Elisabeth Guillaume, Michael Affolter

  • 1Department of Fundamental Microbiology, Faculty of Biology and Medicine, University of Lausanne, CH-1015 Lausanne, Switzerland.

Rapid Communications in Mass Spectrometry : RCM
|April 22, 2006
PubMed
Summary

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A novel sulfanilic acid tagging method improves isotopic coding for carboxylic groups in proteomics. This approach offers better mass shifts and simplified fragmentation, enhancing peptide quantification and C-terminal identification.

Area of Science:

  • Proteomics
  • Analytical Chemistry
  • Biochemistry

Background:

  • Differential isotopic coding of carboxylic groups is crucial for quantitative proteomics.
  • Existing methods using methanol esterification or O-18 labeling have limitations like chromatographic separation and small mass shifts.

Purpose of the Study:

  • To develop a new, improved tagging approach for differential isotopic coding of carboxylic groups.
  • To overcome the limitations of existing methods for enhanced peptide quantification and identification.

Main Methods:

  • Developed a novel tagging strategy using sulfanilic acid, synthesized in a heavy (C-13) form.
  • Applied the sulfanilic acid tag to carboxylic groups, enabling specific derivatization.
  • Utilized matrix-assisted laser desorption/ionization (MALDI) and electrospray ionization (ESI) for analysis.

Related Experiment Videos

  • Employed GluC as a proteolytic enzyme for specific C-terminal peptide identification.

    • Main Results:

    • The sulfanilic acid method provides a significant 6 Da mass shift with no chromatographic shift.
    • Simplified peptide fragmentation in MALDI due to sulfonate group charge fixation at the C-terminus.
    • Reproducible quantification within an order of magnitude.
    • Successful specific identification of C-terminal peptides.

    Conclusions:

    • Sulfanilic acid tagging is a simple, specific, and robust method for quantitative proteomics.
    • This approach enhances isotopic separation and simplifies analysis compared to previous methods.
    • The method facilitates accurate C-terminal peptide identification and improves overall sample analysis efficiency.