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Related Concept Videos

Detergent Purification of Membrane Proteins01:18

Detergent Purification of Membrane Proteins

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Detergents are used to purify the integral proteins of the membrane. The hydrophobic portion of the detergent can replace membrane phospholipids while solubilizing the membrane proteins. When detergent monomers reach a specific concentration in a solution called critical micelle concentration (CMC), they form micelles. Above CMC, the concentration of the detergent monomers remains in equilibrium with the micelle. The number of detergent monomers present in the CMC varies for each detergent, and...
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Organic Solvent-Based Protein Precipitation for Robust Proteome Purification Ahead of Mass Spectrometry
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Dissolving capability difference based sequential extraction: A versatile tool for in-depth membrane proteome

Fei Fang1, Qun Zhao2, Xiao Li2

  • 1Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Science, National Chromatographic Research and Analysis Center, 457 Zhongshan Road, Dalian 116023, China; Graduate School of Chinese Academy of Sciences, Beijing 100039, China.

Analytica Chimica Acta
|December 15, 2016
PubMed
Summary
This summary is machine-generated.

This study introduces a novel sequential extraction method for membrane protein profiling. The advanced technique successfully identified a comprehensive set of membrane proteins, including previously missing ones, from HeLa cells.

Keywords:
Membrane proteome profilingMissing proteinsSample preparationSequential extraction

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Area of Science:

  • Proteomics
  • Cell Biology
  • Biochemistry

Background:

  • Membrane proteins are crucial for cellular functions and drug discovery.
  • Analyzing membrane proteins is challenging due to hydrophobicity and interference from abundant soluble proteins.

Purpose of the Study:

  • To develop and apply an effective sample preparation strategy for comprehensive membrane proteome profiling.
  • To identify a large number of membrane proteins, including low-abundance and hydrophobic ones, from HeLa cells.

Main Methods:

  • A sequential protein extraction strategy using reagents with increasing dissolving power.
  • Nano-liquid chromatography-tandem mass spectrometry (nano-RPLC-ESI-MS/MS) analysis.
  • Application of the method to HeLa cell line.

Main Results:

  • The developed strategy identified 5553 membrane proteins (4419 gene products), with 2573 proteins (2183 gene products) possessing transmembrane domains.
  • This represents the most comprehensive membrane proteome dataset for HeLa cells to date.
  • 110 identified membrane proteins were found on the neXtProt database's 'missing proteins' list.

Conclusions:

  • The sequential extraction strategy significantly enhances the identification of hydrophobic and low-abundance membrane proteins.
  • This approach provides a powerful tool for tackling the complex task of membrane protein identification and profiling.
  • The findings contribute to a deeper understanding of cellular signaling and potential drug targets.