TITLE

Quantitative mass spectrometry in proteomics: a critical review

AUTHOR(S)
Bantscheff, Marcus; Schirle, Markus; Sweetman, Gavain; Rick, Jens; Kuster, Bernhard
PUB. DATE
October 2007
SOURCE
Analytical & Bioanalytical Chemistry;Oct2007, Vol. 389 Issue 4, p1017
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
The quantification of differences between two or more physiological states of a biological system is among the most important but also most challenging technical tasks in proteomics. In addition to the classical methods of differential protein gel or blot staining by dyes and fluorophores, mass-spectrometry-based quantification methods have gained increasing popularity over the past five years. Most of these methods employ differential stable isotope labeling to create a specific mass tag that can be recognized by a mass spectrometer and at the same time provide the basis for quantification. These mass tags can be introduced into proteins or peptides (i) metabolically, (ii) by chemical means, (iii) enzymatically, or (iv) provided by spiked synthetic peptide standards. In contrast, label-free quantification approaches aim to correlate the mass spectrometric signal of intact proteolytic peptides or the number of peptide sequencing events with the relative or absolute protein quantity directly. In this review, we critically examine the more commonly used quantitative mass spectrometry methods for their individual merits and discuss challenges in arriving at meaningful interpretations of quantitative proteomic data. [Figure not available: see fulltext.]
ACCESSION #
26748307

 

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