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Related Concept Videos

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

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...

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Related Experiment Video

Updated: Jul 13, 2026

Low Molecular Weight Protein Enrichment on Mesoporous Silica Thin Films for Biomarker Discovery
13:00

Low Molecular Weight Protein Enrichment on Mesoporous Silica Thin Films for Biomarker Discovery

Published on: April 17, 2012

Targeted protein quantitation and profiling using PVDF affinity probe and MALDI-TOF MS.

Shu-Hua Chen1, Hsin-Kai Liao, Chih-Yang Chang

  • 1Institute of Chemistry, Academia Sinica, Taipei, Taiwan, ROC.

Proteomics
|August 7, 2007
PubMed
Summary

Researchers developed a novel PVDF membrane method for rapid protein identification in plasma. This technique successfully quantified and screened for specific proteins in gastric cancer patients, revealing key biomarkers.

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Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
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Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

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Last Updated: Jul 13, 2026

Low Molecular Weight Protein Enrichment on Mesoporous Silica Thin Films for Biomarker Discovery
13:00

Low Molecular Weight Protein Enrichment on Mesoporous Silica Thin Films for Biomarker Discovery

Published on: April 17, 2012

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
09:35

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

Area of Science:

  • Proteomics
  • Biomarker Discovery
  • Clinical Diagnostics

Background:

  • Identifying specific proteins in complex biological fluids is crucial for proteomic research.
  • Existing methods for protein quantitation and profiling can be time-consuming and complex.
  • There is a need for rapid, effective, and highly specific platforms for target identification.

Purpose of the Study:

  • To develop a simple, effective, and rapid method for protein quantitation and profiling using antibody-immobilized PVDF membranes.
  • To selectively isolate, enrich, and identify targeted plasma proteins (SAP, SAA, CRP) from human plasma.
  • To apply the method for rapid quantitation and variant screening of SAP, SAA, and CRP in healthy individuals and gastric cancer patients.

Main Methods:

  • Utilized antibody-immobilized Polyvinylidene fluoride (PVDF) membranes for selective protein capture via antibody-antigen interactions.
  • Employed Matrix-Assisted Laser Desorption/Ionization-Time of Flight Mass Spectrometry (MALDI-TOF MS) for direct on-probe identification without elution.
  • Performed triplexed on-probe quantitative analysis and variant mass profiling.

Main Results:

  • Successfully isolated and identified targeted plasma proteins (serum amyloid P, serum amyloid A, C-reactive protein) from human plasma.
  • Revealed significant overexpression of C-reactive protein (CRP) and serum amyloid A (SAA) in gastric cancer patients.
  • Identified a high occurrence of de-sialic acid serum amyloid P (SAP) in gastric cancer patients, indicating post-translational modifications.

Conclusions:

  • The developed antibody-immobilized PVDF membrane method offers a rapid, effective, and specific platform for proteomic analysis in complex biofluids.
  • The methodology is suitable for rapid quantitation, variant screening, and biomarker discovery in clinical proteomics, particularly for diseases like gastric cancer.
  • The ease of probe preparation and compatibility with MALDI-TOF MS make this a versatile approach for target protein characterization and functional proteomics.