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Related Concept Videos

Mass Analyzers: Common Types01:19

Mass Analyzers: Common Types

The quadrupole mass analyzer consists of four cylindrical metal rods arranged in a diamond carrying a DC voltage and a radio-frequency AC voltage. The motion of ions through the quadrupole depends on the field strength, causing only ions of a certain m/z to resonate successfully and strike the detector at a given field strength. Though the transmission rate for these analyzers is high, the exact elemental composition of the sample is not determined because of low resolution; however, they are...
Inductively Coupled Plasma-Mass Spectrometry (ICP-MS): Interferences01:20

Inductively Coupled Plasma-Mass Spectrometry (ICP-MS): Interferences

Inductively coupled plasma–mass spectrometry (ICP–MS) is a highly selective and sensitive technique for accurate elemental analysis. Though the analysis of ICP–MS mass spectra is comparatively straightforward, it is affected by spectroscopic and non-spectroscopic interferences. Spectroscopic interferences arise when the plasma contains ionic species with an m/z value the same as the analyte ion. Spectroscopic interference can be categorized as isobaric, polyatomic ions, and refractory oxide ion...
Mass Analyzers: Overview01:13

Mass Analyzers: Overview

The mass analyzer is a crucial component of the mass spectrometer. In the ionization chamber, the vaporized sample is bombarded with a high-energy electron beam to generate a radical cation and further fragment into neutral molecules, radicals, and cations. A series of negatively charged accelerator plates accelerate the cations into the mass analyzer. The mass analyzer separates ions according to their mass-to-charge (m/z) ratios and then directs them to the detector. The common types of mass...
Atomic Absorption Spectroscopy: Interference01:25

Atomic Absorption Spectroscopy: Interference

Interference leads to systematic error in atomic absorption (AA) measurements by enhancing or diminishing the analytical signal or the background. These interferences can be grouped into three main categories: spectral interference, chemical interference, and physical interference.
Spectral interference occurs when signals from other elements or molecules overlap with the analyte signal, falsely elevating or masking the analyte's absorbance. This interference can be corrected using Zeeman,...
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...

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Related Experiment Video

Updated: May 8, 2026

Experimental Methods for Trapping Ions Using Microfabricated Surface Ion Traps
11:45

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Published on: August 17, 2017

iTRAQ analysis with Paul ion trap-obstacle solved.

Anna Drabik1, Anna Bodzoń-Kułakowska, Piotr Suder

  • 1Department of Biochemistry and Neurobiology, AGH University of Science and Technology , Mickiewicza 30 Ave, 30-059 Kraków, Poland.

Journal of Proteome Research
|September 3, 2013
PubMed
Summary

Ion trap mass spectrometers can now quantify peptides using isobaric tags (iTRAQ) despite low mass cutoff limitations. This approach enhances proteomic analysis on widely available instruments.

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Area of Science:

  • Analytical Chemistry
  • Biochemistry
  • Proteomics

Background:

  • Ion trap mass spectrometers offer high performance and affordability.
  • A key limitation of ion traps is their low mass cutoff in MS(n) analysis.
  • This limitation hinders the identification of small molecules and quantification using isobaric tags.

Purpose of the Study:

  • To present a method for quantitative proteomic analysis using isobaric tags on ion trap mass spectrometers.
  • To overcome the low mass cutoff limitation of ion traps for specific applications.
  • To demonstrate the utility of isobaric tags for relative and absolute quantification.

Main Methods:

  • Utilized isobaric tags for relative and absolute quantification labeling (iTRAQ).
  • Employed typical, widely available ion trap mass spectrometry devices.
  • Used manufacturer's software for data analysis.
  • Performed analyses of standard proteins labeled with isobaric tags at various concentration ratios.

Main Results:

  • The presented approach enables quantitative proteomic analysis using ion trap devices.
  • Demonstrated the feasibility of using isobaric tags (iTRAQ) for quantification despite the low mass cutoff.
  • Series of analyses confirmed the quantitative capabilities of the method.

Conclusions:

  • The developed approach expands the application of ion trap mass spectrometers in quantitative proteomics.
  • Isobaric tag labeling (iTRAQ) can be effectively used with ion traps for small molecule and peptide quantification.
  • This method provides a cost-effective solution for quantitative proteomic studies using common instrumentation.