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Related Concept Videos

Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
Mass Spectrometry: Complex Analysis01:21

Mass Spectrometry: Complex Analysis

Mass spectrometry is an important technique for the identification of pure compounds. However, it has some limitations for the analysis of complex mixtures, often due to excessive fragmentation making the spectrum too complicated to decipher. Mass spectrometry can be combined with suitable separation methods in sequence, forming hyphenated methods, which are useful in the analysis of complex mixtures.
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...
MALDI-TOF Mass Spectrometry01:19

MALDI-TOF Mass Spectrometry

Mass spectrometry is a powerful characterization technique that can identify and separate a wide variety of compounds ranging from chemical to biological entities, based on their mass-to-charge ratio (m/z). The instruments that allow this detection, known as mass spectrometers, have three components: an ion source, a mass analyzer, and a detector. These spectrometers differ based on the nature of their ion source and analyzers.Matrix-assisted laser desorption ionization (MALDI) is a commonly...

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Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification
09:04

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Published on: August 17, 2015

Mass spectrometry-based approaches toward absolute quantitative proteomics.

Keiji Kito1, Takashi Ito

  • 1Department of Computational Biology, Graduate School of Frontier Sciences, University of Tokyo, Kashiwa 277-8561, Japan.

Current Genomics
|May 20, 2009
PubMed
Summary

Mass spectrometry enables large-scale protein cataloging and quantification in proteomics. Recent advances in stable isotope labeling and label-free methods are driving absolute proteome quantification, offering deeper biological insights.

Keywords:
Quantitative proteomicsabsolute quantificationlabel-free.mass spectrometrystable isotope labeling

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Last Updated: Jun 23, 2026

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification
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Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Molecular Biology

Background:

  • Mass spectrometry is a cornerstone of proteomics, enabling large-scale protein identification.
  • Stable isotope labeling techniques have advanced relative protein quantification.
  • Absolute quantification of the proteome is emerging as a critical frontier.

Purpose of the Study:

  • To review mass spectrometry-based methods for absolute proteome quantification.
  • To discuss the implications of these advanced quantification strategies.
  • To highlight progress in both labeled and label-free approaches.

Main Methods:

  • Review of stable isotope labeling techniques (chemical and metabolic).
  • Analysis of strategies using isotope-labeled concatenated peptide standards.
  • Examination of label-free quantification methods based on peptide counts.

Main Results:

  • Stable isotope labeling facilitates routine relative quantification of protein abundance.
  • Concatenated peptide standards enable absolute or stoichiometric proteome quantification.
  • Label-free methods show significant progress for proteome quantification.

Conclusions:

  • Mass spectrometry-based absolute proteome quantification is becoming increasingly feasible.
  • These advancements provide valuable insights into proteome-wide alterations.
  • The reviewed methods are crucial for understanding complex biological systems.