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Article
Quantitative Proteomics Employing Primary Amine Affinity Tags
Journal of Biomolecular Techniques
  • Van M. Hoang
  • Thomas P. Conrads
  • Timothy D. Veenstra, Cedarville University
  • Josip Blonder
  • Atsushi Terunuma
  • Jonathan C. Vogel
  • Robert J. Fisher
Document Type
Article
Publication Date
9-1-2003
PubMed ID
13678152
PubMed Central® ID
PMC2279946
Abstract

A proteomics-based method using stable isotope labeling to assess the relative abundance of peptides or proteins is described. Bradykinin and carbonic anhydrase were labeled with sulfosuccinimidyl-2-(biotinamido) ethyl-1,3-dithiopropionate, a membrane impermeant reagent that is reactive with primary amines. Specificity of the label to primary amines was demonstrated using tandem mass spectrometry. Also, relative quantitation was achieved by secondary labeling with natural isotopic abundance and stable isotope-labeled methyl iodide. We believe this to be an effective stable isotope-labeling method for quantitative proteomics.

Keywords
  • Amines,
  • amino acid sequence,
  • carbonic anhydrases,
  • lysine,
  • proteomics,
  • spectrometry,
  • mass
Citation Information
Van M. Hoang, Thomas P. Conrads, Timothy D. Veenstra, Josip Blonder, et al.. "Quantitative Proteomics Employing Primary Amine Affinity Tags" Journal of Biomolecular Techniques Vol. 14 Iss. 3 (2003) p. 216 - 223 ISSN: 1524-0215
Available at: http://works.bepress.com/timothy-veenstra/327/