Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Tandem Mass Spectrometry

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...

Proteomics

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

Peptide Identification Using Tandem Mass Spectrometry

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: Overview

Mass Spectrometry: Overview

Mass spectrometry is an analytical technique used to determine the molecular mass and molecular formula of a compound. The basic principle of mass spectrometry is to generate ions from the analyte molecule and measure these ion abundances against their molecular mass. One common type of ionization, known as electron ionization or EI, bombards the analyte molecules in the gas phase with high-energy electron beams. The electron beams displace an electron from the molecule and leave behind a...

MALDI-TOF Mass Spectrometry

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...

Mass Spectrometry: Complex Analysis

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

Blood Cancer Clinical Trials Long-term Follow-up Using Integrated Healthcare Systems Data (BLISS): protocol for a data-linkage study integrating randomised clinical trials with national healthcare systems data.

BMJ open·2026

Same author

The density of tumour infiltrating lymphocytes in oesophago-gastric cancer varies with disease stage, geographical region and treatment: a post hoc analysis of nine phase III clinical trials.

Gastric cancer : official journal of the International Gastric Cancer Association and the Japanese Gastric Cancer Association·2026

Same author

Patient-reported health-related quality of life in previously untreated chronic lymphocytic leukaemia: Results from the randomised phase 3 FLAIR trial comparing ibrutinib-rituximab versus fludarabine-cyclophosphamide-rituximab.

British journal of haematology·2026

Same author

Associations of Creatinine Muscle Index with markers of sarcopenia and mortality in chronic kidney disease: A prospective cohort study.

PLoS medicine·2026

Same author

Sex-Associated Biomarker Differences in CKD Progression and Mortality.

Clinical journal of the American Society of Nephrology : CJASN·2026

Same author

Biomarker Prediction of Delayed Graft Function and Prognosis Post-Kidney Transplantation.

Kidney international reports·2026

Search research articles

Related Experiment Video

Updated: Jul 9, 2026

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

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

Published on: November 15, 2017

Proteomic profiling using mass spectrometry--does normalising by total ion current potentially mask some biological

David A Cairns¹, Douglas Thompson, David N Perkins

¹Clinical and Biomedical Proteomics Group, Cancer Research UK Clinical Centre, Leeds Institute of Molecular Medicine, St. James's University Hospital, Leeds, UK.

|December 21, 2007

Summary

Total Ion Chromatogram (TIC) normalization in mass spectrometry (MS) data may obscure biological differences in serum profiles. Researchers found significant intergroup differences in normalization factors, warranting careful evaluation of this common data processing technique.

More Related Videos

Navigating the Mass Spectrometry-Based Proteomic Data Using Free Computational Tools

Navigating the Mass Spectrometry-Based Proteomic Data Using Free Computational Tools

Published on: August 19, 2025

Related Experiment Videos

Last Updated: Jul 9, 2026

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

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

Published on: November 15, 2017

Navigating the Mass Spectrometry-Based Proteomic Data Using Free Computational Tools

Navigating the Mass Spectrometry-Based Proteomic Data Using Free Computational Tools

Published on: August 19, 2025

Area of Science:

Biochemistry
Analytical Chemistry
Proteomics

Background:

Data normalization is crucial for minimizing technical variation in comparative sample analysis.
Surface-Enhanced Laser Desorption/Ionization (SELDI) mass spectrometry (MS) is a common technique for analyzing complex biological samples.
Total Ion Chromatogram (TIC) normalization is frequently applied to MS data to account for instrument sensitivity variations.

Purpose of the Study:

To investigate the impact of TIC normalization on comparative analysis of SELDI data.
To determine if TIC normalization can inadvertently mask biological variations between sample groups.
To assess the suitability of TIC normalization for serum proteomic profiling.

Main Methods:

Utilized SELDI data as a model system for evaluating normalization effects.
Applied TIC normalization to serum proteomic profiles.
Analyzed normalization factors to identify intergroup differences.
Investigated potential experimental factors contributing to observed variations.

Main Results:

Significant intergroup differences in normalization factors were observed in serum profiles.
These differences could not be attributed to known experimental or technical factors.
The findings suggest that TIC normalization may normalize biological signals in certain contexts.

Conclusions:

TIC normalization, while common for MS data, may obscure genuine biological differences in comparative analyses.
Systematic evaluation of TIC normalization's impact on biological variation is necessary, particularly for serum proteomic studies.
Researchers should carefully consider alternative normalization strategies or validate TIC normalization's appropriateness for their specific datasets.