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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...
Peptide Identification Using Tandem Mass Spectrometry01:33

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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...

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Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted 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

Large molecule bioanalysis using Q-TOF without predigestion and its data processing challenges.

Suma Ramagiri1, Fabio Garofolo

  • 1AB Sciex, Concord, ON, Canada.

Bioanalysis
|March 14, 2012
PubMed
Summary
This summary is machine-generated.

High-resolution mass spectrometry (MS) enables sensitive quantification of intact peptides and small proteins, offering an alternative to traditional methods. This approach enhances selectivity and sensitivity without requiring tryptic digestion for bioanalysis.

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A Strategy for Sensitive, Large Scale Quantitative Metabolomics
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A Strategy for Sensitive, Large Scale Quantitative Metabolomics
14:18

A Strategy for Sensitive, Large Scale Quantitative Metabolomics

Published on: May 27, 2014

Area of Science:

  • Analytical Chemistry
  • Biochemistry
  • Biotechnology

Background:

  • Liquid chromatography-mass spectrometry (LC-MS) is an emerging alternative to ligand-binding assays for bioanalysis.
  • Traditional LC-MS for large molecules involves tryptic digestion into peptides.
  • High-resolution MS enhances selectivity and sensitivity in peptide quantification.

Purpose of the Study:

  • To evaluate LC-MS for quantifying intact peptides and small proteins.
  • To demonstrate the feasibility of intact molecule quantification without enzymatic digestion.
  • To optimize data processing and quantification parameters for LC-MS methods.

Main Methods:

  • Utilized high-resolution mass spectrometry (MS) instruments.
  • Employed time-of-flight MS (TOF-MS) and TOF-MS/MS scan modes.
  • Quantified intact peptides and small proteins without tryptic digestion.

Main Results:

  • Demonstrated successful quantification of intact peptides and small proteins, including MUC5AC-13, hepcidin, calcitonin, and lysozyme.
  • Identified optimal parameters for quantification method development in LC-MS.
  • Showcased improved selectivity and sensitivity using TOF-MS and TOF-MS/MS.

Conclusions:

  • LC-MS can quantify intact peptides and small proteins without tryptic digestion.
  • High-resolution MS, particularly TOF-MS/MS, improves selectivity and sensitivity in bioanalysis.
  • Optimized methods enhance the viability of LC-MS for large molecule bioanalysis.