The use of stable isotopes as internal standards in mass spectrometry has opened a new era for quantitative proteomics. Depending on the point at which the label is introduced, most procedures can be classified as in vivo labeling, in vitro pre-digestion labeling or in vitro post-digestion labeling.
Advancements in plant proteomics using quantitative mass spectrometry
β Scribed by Silke Oeljeklaus; Helmut E. Meyer; Bettina Warscheid
- Publisher
- Elsevier
- Year
- 2009
- Tongue
- English
- Weight
- 327 KB
- Volume
- 72
- Category
- Article
- ISSN
- 1874-3919
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
The high-throughput identification and accurate quantification of proteins are essential components of proteomic strategies for studying cellular functions and processes. Techniques that are largely based on stable isotope protein or peptide labeling and automated tandem mass spectrometry are increa
The most demanding problems in proteomics continue to challenge modern mass spectrometry. Recent developments in instrument design have led to lower limits of detection, while new ion activation techniques and improved understanding of gas-phase ion chemistry have enhanced the capabilities of tandem
## Abstract | ββI. | Introduction | 182 | | βII. | Relative Quantitation | 184 | | | A.ββ2βD Gel Electrophoresis | 184 | | | B.ββMetabolic Isotopic Labeling | 185 | | | ββββ1.ββ^15^N | 185 | | | ββββ2.ββ^13^C Enrichment and Depletion | 185 | | | ββββ3.ββSelect Isotopic Amino Acid Incorporation
## Abstract The proteome, defined as an organism's proteins and their actions, is a highly complex endβeffector of molecular and cellular events. Differing amounts of proteins in a sample can be indicators of an individual's health status; thus, it is valuable to identify key proteins that serve as