Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

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...
Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

Tandem mass spectrometry is a technique that uses multiple mass analyzers in series to obtain a higher selectivity and reduce chemical noise during analyte detection. Instruments with multiple analyzers separated by an interaction cell enable secondary fragmentation and selected study of the fragment ions.Secondary fragmentations occur in the interaction cell and can be induced by various factors. Fragmentation induced by collision with inert gases, such as N2, Ar, He, etc., is called...
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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Result Interpretation in Skewed Populations-Are Common Reference Intervals Inadequate?

The journal of applied laboratory medicine·2026
Same author

Big Data Approach to Assessment of an Aldosterone-Renin Ratio for Detection of Potential Surgical Cases of Primary Aldosteronism.

Hypertension (Dallas, Tex. : 1979)·2026
Same author

Implications of specific ion effects on salt-induced proteome precipitation in organic solvent.

Analytica chimica acta·2026
Same author

Seated Saline Suppression Test for Lateralizing Primary Aldosteronism.

Hypertension (Dallas, Tex. : 1979)·2026
Same author

Outcomes After Unilateral Adrenalectomy in Asymmetrical Bilateral Primary Aldosteronism.

Hypertension (Dallas, Tex. : 1979)·2025
Same author

SDS Depletion from Intact Membrane Proteins by KCl Precipitation Ahead of Mass Spectrometry Analysis.

Proteomes·2025
Same journal

Proteomic Profiling of Endothelial Cells Under Laminar Shear Stress Confirms the Importance of KLF4 in the Regulation of Membrane Protein Expression Compared to Oscillatory Flow.

Journal of proteome research·2026
Same journal

Identification of Age-Associated Circulating Proteins and Lipids in 3800 Comorbidity-Enriched Older Adults from Japan-Based Cohorts Using Olink Assays and MRM Mass Spectrometry.

Journal of proteome research·2026
Same journal

Molecular Solution to the Paradox of Ancient Brain Preservation.

Journal of proteome research·2026
Same journal

From Method-Defined Signals to Reference Measurement Procedures: Two Decades of Mass Spectrometry-Based ProGRP Quantification.

Journal of proteome research·2026
Same journal

Proteomic Profiling of Extracellular Vesicle-Enriched Plasma Using Mag-Net for Biomarker Discovery in Pancreatic Ductal Adenocarcinoma.

Journal of proteome research·2026
Same journal

Computationally Efficient Bayesian Estimation of Graphical Networks for Omics Data.

Journal of proteome research·2026
See all related articles

Related Experiment Video

Updated: May 7, 2026

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
10:37

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

Published on: November 15, 2017

Dual LC-MS platform for high-throughput proteome analysis.

Dennis J Orton1, Mark J Wall, Alan A Doucette

  • 1Department of Pathology, Dalhousie University , 11th Floor Tupper Medical Building, Room 11B, Halifax, NS B3H 4R2, Canada.

Journal of Proteome Research
|October 5, 2013
PubMed
Summary
This summary is machine-generated.

A new dual-column interface for liquid chromatography-mass spectrometry (LC-MS) nearly doubles experimental throughput. This parallel chromatography system enhances proteome analysis efficiency, identifying significantly more peptides and proteins per hour.

More Related Videos

2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes
08:23

2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes

Published on: August 6, 2018

Related Experiment Videos

Last Updated: May 7, 2026

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
10:37

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

Published on: November 15, 2017

2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes
08:23

2 in 1: One-step Affinity Purification for the Parallel Analysis of Protein-Protein and Protein-Metabolite Complexes

Published on: August 6, 2018

Area of Science:

  • Analytical Chemistry
  • Biochemistry
  • Proteomics

Background:

  • Liquid chromatography-mass spectrometry (LC-MS) is a key technique in proteomics.
  • Improving the throughput of LC-MS experiments is crucial for large-scale proteome analysis.
  • Existing LC-MS methods face limitations in speed and efficiency.

Purpose of the Study:

  • To develop and evaluate a dual-column interface for parallel chromatography to enhance LC-MS throughput.
  • To assess the impact of the dual-column system on proteome analysis efficiency and data quality.
  • To investigate methods for maximizing throughput gains in LC-MS experiments.

Main Methods:

  • Implementation of a dual-column interface with a high-voltage switch for sequential column operation.
  • Utilizing two capillary columns and nanospray emitters in parallel with a single mass spectrometer.
  • Application to GeLC (Gel-LC) analysis of an E. coli extract, with variations in gel slicing and gradient length.

Main Results:

  • The dual-column system nearly doubles the LC-MS duty cycle.
  • Intercolumn variability showed no meaningful difference in proteome analysis.
  • Analysis on the dual-column platform resulted in a 26% increase in peptides identified per hour and a 24% increase in proteins.
  • A ~50% increase in total proteins and peptides identified was achieved using the dual LC-MS platform.

Conclusions:

  • The dual-column interface significantly improves LC-MS throughput without compromising data quality.
  • This parallel chromatography approach offers a substantial increase in proteomic identification efficiency.
  • The developed system provides a valuable tool for accelerating large-scale proteome studies.