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Related Concept Videos

SDS-PAGE01:27

SDS-PAGE

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Gel electrophoresis is a method that separates biological macromolecules like nucleic acids or proteins by forcing them to pass through a gel matrix under an electric field.
A variation of gel electrophoresis, termed  polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact...
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Related Experiment Video

Updated: Apr 30, 2026

Multiplexed Fluorescent Microarray for Human Salivary Protein Analysis Using Polymer Microspheres and Fiber-optic Bundles
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Multiplexed Fluorescent Microarray for Human Salivary Protein Analysis Using Polymer Microspheres and Fiber-optic Bundles

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Decrease of dynamic range of proteins in human plasma by ampholine immobilized polymer microspheres.

Nan Deng1, Guijie Zhu2, Yuanbo Chen1

  • 1National Chromatographic Research and Analysis Center, Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China; Graduate School of the Chinese Academy of Sciences, Beijing 100039, China.

Analytica Chimica Acta
|May 6, 2014
PubMed
Summary

A new method using ampholine immobilized polymer microspheres (ampholine@PM) effectively fractionates human plasma proteins. This reduces the protein dynamic range, improving the identification of low-abundance proteins for deeper proteome coverage.

Keywords:
AmpholineFractionationHuman plasmaProtein dynamic range

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Area of Science:

  • Proteomics
  • Biochemistry
  • Analytical Chemistry

Background:

  • The human plasma proteome is characterized by a vast dynamic range of protein concentrations.
  • This wide range poses significant challenges for identifying low-abundance proteins using mass spectrometry-based proteomics.
  • Effective sample pretreatment methods are crucial for overcoming these limitations.

Purpose of the Study:

  • To develop and evaluate a novel protein sample pretreatment method for fractionating intact proteins.
  • To reduce the dynamic range of the human plasma proteome.
  • To enhance the identification and coverage of low-abundance proteins in plasma.

Main Methods:

  • Development of ampholine immobilized polymer microspheres (ampholine@PM) for protein fractionation.
  • Incubation of human plasma with ampholine@PM, followed by sequential desorption using different solutions (2M NaCl, 100mM glycine-HCl, 30% acetonitrile/0.1% TFA).
  • On-particle digestion of captured proteins and subsequent analysis using MuPIT (Mass-Unbiased Protein Identification Technology).

Main Results:

  • SDS-PAGE confirmed a significant reduction in the protein dynamic range across the three fractions compared to native plasma.
  • The ampholine@PM treatment resulted in a 75% increase in the number of identified plasma proteins.
  • Spectral counts of high-abundance proteins decreased by 37.6-97.2%, while the number of identified low-abundance proteins (<100 ng/mL) increased from 4 to 17.

Conclusions:

  • Ampholine@PM is an effective method for fractionating intact proteins in human plasma.
  • This fractionation significantly reduces protein abundance dynamic range, enabling deeper proteome coverage.
  • The developed method facilitates the identification of low-abundance proteins, advancing plasma proteomic research.