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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...
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...
Rapid Identification of Pathogens01:25

Rapid Identification of Pathogens

MALDI-TOF MS has transformed clinical microbiology by offering a rapid and reliable method for pathogen identification. The traditional approach to microbial identification typically involves time-consuming culture techniques and biochemical tests, which can delay the initiation of appropriate antimicrobial therapy. MALDI-TOF MS avoids these delays by using characteristic ribosomal protein mass patterns of microbial cells, enabling accurate species-level identification within minutes.Principle...

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Related Experiment Video

Updated: Jul 17, 2026

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

Published on: April 17, 2012

Trypsin-linked copolymer MALDI chips for fast protein identification.

Alfredo J Ibañez1, Alexander Muck, Vincentius Halim

  • 1Mass Spectrometry Research Group, Max Planck Institute for Chemical Ecology, Hans-Knöll-Strasse 8, 07745 Jena, Germany.

Journal of Proteome Research
|January 25, 2007
PubMed
Summary

New enzyme-linked polymer chips enable integrated proteomic sample preparation and measurement. This novel approach simplifies protein analysis, identifying four proteins from a mixture with high efficiency.

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Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor
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Last Updated: Jul 17, 2026

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

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Published on: April 17, 2012

The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes
09:47

The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes

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Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor
09:49

Fast Enzymatic Processing of Proteins for MS Detection with a Flow-through Microreactor

Published on: April 6, 2016

Area of Science:

  • Biochemistry
  • Materials Science
  • Analytical Chemistry

Background:

  • Proteomic sample preparation often involves multiple time-consuming steps.
  • Developing integrated platforms for efficient protein analysis is crucial for high-throughput screening.

Purpose of the Study:

  • To fabricate and characterize novel trypsin-linked copolymer chips for integrated proteomic sample preparation and measurement.
  • To demonstrate the chips' efficiency in enzymatic protein digestion and subsequent peptide mass fingerprinting.

Main Methods:

  • Fabrication of poly(methyl methacrylate-co-2-amino-ethyl methacrylamide) chips using atmospheric molding.
  • Covalent immobilization of trypsin onto the chip surface via a succinimidyl ester linker.
  • On-chip enzymatic digestion of individual proteins and protein mixtures.
  • Peptide mass fingerprinting using MALDI-TOF and protein database searching.

Main Results:

  • Successful fabrication of trypsin-linked copolymer chips via a simple atmospheric molding protocol.
  • Demonstrated superior performance for enzymatic digestion of proteins (500 fmol) across a 5-60 kDa size range.
  • Accurate identification of all four proteins (cytochrome C, BSA, hemoglobin, myoglobin) from a mixture after on-chip digestion and peptide mass fingerprinting.

Conclusions:

  • The novel enzyme-linked chips offer an efficient integrated solution for proteomic sample preparation and analysis.
  • This approach significantly minimizes sample handling time and enhances analytical information.
  • The concept is adaptable for high-throughput enzyme activity screening and protein processing applications.