Pharmaceutical Sciences Faculty Publications
Quantitative Proteomics Employing Primary Amine Affinity Tags
Document Type
Article
Publication Date
9-1-2003
Journal Title
Journal of Biomolecular Techniques
ISSN
1524-0215
Volume
14
Issue
3
First Page
216
Last Page
223
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
Recommended Citation
Hoang, Van M.; Conrads, Thomas P.; Veenstra, Timothy D.; Blonder, Josip; Terunuma, Atsushi; Vogel, Jonathan C.; and Fisher, Robert J., "Quantitative Proteomics Employing Primary Amine Affinity Tags" (2003). Pharmaceutical Sciences Faculty Publications. 488.
https://digitalcommons.cedarville.edu/pharmaceutical_sciences_publications/488