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Comparative proteomics based on stable isotope labeling and affinity selection
Author(s) -
Regnier Fred E.,
Riggs Larry,
Zhang Roujian,
Xiong Li,
Liu Peiran,
Chakraborty Asish,
Seeley Erin,
Sioma Cathy,
Thompson Robert A.
Publication year - 2002
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/jms.290
Subject(s) - chemistry , computational biology , proteomics , posttranslational modification , peptide , mass spectrometry , isotopic labeling , quantitative proteomics , tandem mass spectrometry , biochemistry , chromatography , gene , biology , organic chemistry , enzyme
Disease, external stimuli (such as drugs and toxins), and mutations cause changes in the rate of protein synthesis, post‐translational modification, inter‐compartmental transport, and degradation of proteins in living systems. Recognizing and identifying the small number of proteins involved is complicated by the complexity of biological extracts and the fact that post‐translational alterations of proteins can occur at many sites in multiple ways. It is shown here that a variety of new tools and methods based on internal standard technology are now being developed to code globally all peptides in control and experimental samples for quantification. The great advantage of these stable isotope‐labeling strategies is that mass spectrometers can rapidly target those proteins that have changed in concentration for further analysis. When coupled to stable isotope quantification, targeting can be further focused through chromatographic selection of peptide classes on the basis of specific structural features. Targeting structural features is particularly useful when they are unique to types of regulation or disease. Differential displays of targeted peptides show that stimulus‐specific markers are relatively easy to identify and will probably be diagnostically valuable tools. Copyright © 2002 John Wiley & Sons, Ltd.