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SDS-PAGE

SDS-PAGE

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 proteins...

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Updated: Jun 3, 2026

Blue Native Polyacrylamide Gel Electrophoresis (BN-PAGE) for Analysis of Multiprotein Complexes from Cellular Lysates

Blue Native Polyacrylamide Gel Electrophoresis (BN-PAGE) for Analysis of Multiprotein Complexes from Cellular Lysates

Published on: February 24, 2011

Low-SDS Blue native PAGE.

Jennifer Klodmann¹, Dagmar Lewejohann, Hans-Peter Braun

¹Institute for Plant Genetics, Faculty of Natural Sciences, Leibniz Universität Hannover, Hannover, Germany.

|March 18, 2011

Summary

This summary is machine-generated.

This study introduces a modified Blue Native PAGE method using low SDS concentrations. This technique allows for reproducible dissection and analysis of protein complex architecture without prior purification.

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Blue Native Polyacrylamide Gel Electrophoresis (BN-PAGE) for Analysis of Multiprotein Complexes from Cellular Lysates

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Published on: February 24, 2011

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Hybrid Clear/Blue Native Electrophoresis for the Separation and Analysis of Mitochondrial Respiratory Chain Supercomplexes

Hybrid Clear/Blue Native Electrophoresis for the Separation and Analysis of Mitochondrial Respiratory Chain Supercomplexes

Published on: May 19, 2019

Area of Science:

Biochemistry
Proteomics
Molecular Biology

Background:

Blue Native Polyacrylamide Gel Electrophoresis (BN-PAGE) is crucial for studying native protein complexes.
Sodium dodecyl sulfate (SDS) is typically avoided in BN-PAGE as it disrupts protein complexes and causes unfolding.

Purpose of the Study:

To develop a modified BN-PAGE procedure enabling controlled dissection of protein complexes.
To investigate the internal architecture of protein complexes using a novel 2-D and 3-D gel electrophoresis system.

Main Methods:

A modified BN-PAGE procedure involving low-SDS treatment of biological samples before native gel electrophoresis.
Application of 2-D BN/SDS-PAGE and a 3-D BN/low-SDS BN/SDS-PAGE system.
Utilizing mitochondrial OXPHOS complexes from Arabidopsis as a model system.

Main Results:

Low SDS concentrations reproducibly dissect protein complexes into defined subcomplexes.
The 2-D BN/SDS-PAGE approach allows systematic investigation of subcomplexes and their subunits.
The 3-D system facilitates structural analysis of individual protein complexes without prior purification.

Conclusions:

Modified BN-PAGE with low SDS offers a powerful tool for dissecting and analyzing protein complex architecture.
This method provides new insights into the structural organization of protein complexes.
The developed system simplifies structural analysis of protein complexes, reducing the need for extensive purification steps.