Quantitative proteomics employing primary amine affinity tags

M. Van Hoang; Thomas P. Conrads; Timothy D. Veenstra; Josip Blonder; Atsushi Terunuma; Jonathan C. Vogel; Robert J. Fisher

Quantitative proteomics employing primary amine affinity tags

M. Van Hoang, Thomas P. Conrads, Timothy D. Veenstra, Josip Blonder, Atsushi Terunuma, Jonathan C. Vogel, Robert J. Fisher

Research output: Contribution to journal › Article › peer-review

22 Scopus citations

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-dithiopro-pionate, 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.

Original language	English
Pages (from-to)	216-223
Number of pages	8
Journal	Journal of Biomolecular Techniques
Volume	14
Issue number	3
State	Published - Sep 2003
Externally published	Yes

Keywords

Proteomics
Stable isotope labeling
Sulfo-NHS-SS-biotin

Cite this

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title = "Quantitative proteomics employing primary amine affinity tags",

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-dithiopro-pionate, 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 = "Proteomics, Stable isotope labeling, Sulfo-NHS-SS-biotin",

author = "{Van Hoang}, M. and Conrads, {Thomas P.} and Veenstra, {Timothy D.} and Josip Blonder and Atsushi Terunuma and Vogel, {Jonathan C.} and Fisher, {Robert J.}",

year = "2003",

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language = "English",

volume = "14",

pages = "216--223",

journal = "Journal of Biomolecular Techniques",

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T1 - Quantitative proteomics employing primary amine affinity tags

AU - Van Hoang, M.

AU - Conrads, Thomas P.

AU - Veenstra, Timothy D.

AU - Blonder, Josip

AU - Terunuma, Atsushi

AU - Vogel, Jonathan C.

AU - Fisher, Robert J.

PY - 2003/9

Y1 - 2003/9

N2 - 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-dithiopro-pionate, 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.

AB - 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-dithiopro-pionate, 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.

KW - Proteomics

KW - Stable isotope labeling

KW - Sulfo-NHS-SS-biotin

UR - http://www.scopus.com/inward/record.url?scp=2342464385&partnerID=8YFLogxK

M3 - Article

C2 - 13678152

AN - SCOPUS:2342464385

SN - 1524-0215

VL - 14

SP - 216

EP - 223

JO - Journal of Biomolecular Techniques

JF - Journal of Biomolecular Techniques

IS - 3

ER -

Quantitative proteomics employing primary amine affinity tags

Abstract

Keywords

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