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

MALDI-TOF Mass Spectrometry01:19

MALDI-TOF Mass Spectrometry

7.6K
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...
7.6K
Matrix-Assisted Laser Desorption Ionization (MALDI)01:08

Matrix-Assisted Laser Desorption Ionization (MALDI)

1.4K
Matrix-assisted laser desorption ionization (MALDI) is a powerful analytical technique used in mass spectrometry. It enables the identification and characterization of various biomolecules, including proteins, peptides, nucleic acids, and carbohydrates. MALDI is an ionization technique, widely employed in biological and medical research, as well as in fields like pharmacology and biochemistry.The analyte of interest, a biomolecule or a mixture of biomolecules, is mixed with a suitable matrix...
1.4K

You might also read

Related Articles

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

Sort by
Same author

Online Deglycosylation of Monomeric Intact Proteins Using the PNGase Rc Immobilized-Enzyme Reactor.

ACS omega·2026
Same author

Biochemical impacts of triazole fungicides on tomato roots and soil enzyme activities.

Journal of environmental science and health. Part. B, Pesticides, food contaminants, and agricultural wastes·2026
Same author

Transcriptome-guided discovery of novel plant-associated genes in a rhizosphere Pseudomonas.

Microbiome·2025
Same author

DigDig: A Software for In-Depth Analysis and Comparison of Proteolytic Digestion.

Analytical chemistry·2025
Same author

[Conditions mimicking acute bacterial skin and soft tissue infections].

Klinicka mikrobiologie a infekcni lekarstvi·2025
Same author

Proof-of-concept MALDI-TOF-MS assay for the detection of Toxin B enzymatic activity in <i>Clostridioides difficile</i> infection.

Microbiology spectrum·2025

Related Experiment Video

Updated: Mar 31, 2026

Analysis of Complex Molecules and Their Reactions on Surfaces by Means of Cluster-Induced Desorption/Ionization Mass Spectrometry
07:53

Analysis of Complex Molecules and Their Reactions on Surfaces by Means of Cluster-Induced Desorption/Ionization Mass Spectrometry

Published on: March 1, 2020

7.9K

Planar Functionalized Surfaces for Direct Immunoaffinity Desorption/Ionization Mass Spectrometry.

Petr Pompach1, Jana Nováková2, Daniel Kavan3

  • 1Institute of Microbiology, v.v.i., Czech Academy of Sciences, Prague, Czech Republic; Faculty of Science, Charles University in Prague, Prague, Czech Republic; AffiPro, s.r.o., Mratin, Czech Republic;

Clinical Chemistry
|October 21, 2015
PubMed
Summary

A new MALDI mass spectrometry method enables rapid haptoglobin phenotyping, crucial for predicting cardiovascular risks in diabetes patients. This technique offers a high-throughput alternative to traditional methods.

More Related Videos

Imaging of Biological Tissues by Desorption Electrospray Ionization Mass Spectrometry
06:21

Imaging of Biological Tissues by Desorption Electrospray Ionization Mass Spectrometry

Published on: July 12, 2013

19.5K
In Situ SIMS and IR Spectroscopy of Well-defined Surfaces Prepared by Soft Landing of Mass-selected Ions
10:22

In Situ SIMS and IR Spectroscopy of Well-defined Surfaces Prepared by Soft Landing of Mass-selected Ions

Published on: June 16, 2014

19.1K

Related Experiment Videos

Last Updated: Mar 31, 2026

Analysis of Complex Molecules and Their Reactions on Surfaces by Means of Cluster-Induced Desorption/Ionization Mass Spectrometry
07:53

Analysis of Complex Molecules and Their Reactions on Surfaces by Means of Cluster-Induced Desorption/Ionization Mass Spectrometry

Published on: March 1, 2020

7.9K
Imaging of Biological Tissues by Desorption Electrospray Ionization Mass Spectrometry
06:21

Imaging of Biological Tissues by Desorption Electrospray Ionization Mass Spectrometry

Published on: July 12, 2013

19.5K
In Situ SIMS and IR Spectroscopy of Well-defined Surfaces Prepared by Soft Landing of Mass-selected Ions
10:22

In Situ SIMS and IR Spectroscopy of Well-defined Surfaces Prepared by Soft Landing of Mass-selected Ions

Published on: June 16, 2014

19.1K

Area of Science:

  • Clinical Chemistry
  • Analytical Chemistry
  • Biotechnology

Background:

  • Haptoglobin phenotype is a key predictor of cardiovascular events in diabetes mellitus patients.
  • Current phenotyping methods (PCR, gel electrophoresis) lack high-throughput capability for clinical applications.
  • Mass spectrometry (MS) offers potential for rapid phenotyping due to mass differences in haptoglobin variants, but requires efficient sample enrichment.

Purpose of the Study:

  • To develop and validate a rapid, high-throughput method for haptoglobin phenotyping using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS).
  • To address the need for efficient serum enrichment techniques for MS-based haptoglobin analysis.

Main Methods:

  • Functionalization of MALDI plates with antihaptoglobin antibody via ambient ion landing.
  • In situ immunoaffinity enrichment of haptoglobin directly on the functionalized MALDI plate.
  • Analysis by MALDI-TOF MS with phenotype determination by embedded software script.

Main Results:

  • MALDI mass spectra clearly identified haptoglobin α subunits at specific m/z values.
  • Analysis of 116 serum samples showed 100% agreement with Western blot, confirming method reliability.
  • The developed method demonstrated efficient MALDI ionization and low nonspecific interactions.

Conclusions:

  • MALDI plates modified with antihaptoglobin antibody via ambient ion landing provide a reliable platform for rapid haptoglobin phenotyping.
  • This immunoaffinity MS approach is suitable for high-throughput clinical applications.
  • The method offers a significant advancement over traditional phenotyping techniques.