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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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Related Experiment Video

Updated: Jun 4, 2026

Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples

Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples

Published on: May 5, 2017

SDS-PAGE Peptide-Mapping Procedure (Cleveland Method).

Richard J Simpson

|March 2, 2011

Summary

This summary is machine-generated.

This study introduces a novel peptide mapping technique using partial protein digestion in solution, followed by separation using SDS-PAGE. This method improves the identification of larger peptide fragments for protein analysis.

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Last Updated: Jun 4, 2026

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Area of Science:

Biochemistry
Proteomics

Background:

Traditional peptide mapping often uses total protein digestion, yielding small peptides that are difficult to analyze.
These small peptides can be poorly fixed in gels, limiting their utility in peptide mapping.

Purpose of the Study:

To present an improved method for peptide mapping of proteins.
To enhance the identification and analysis of peptide fragments.

Main Methods:

Partial hydrolysis of proteins in solution.
Separation of resulting peptide fragments using SDS-PAGE (Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis).

Main Results:

The method yields a significant number of large peptides.
These larger peptides are readily identifiable using SDS-PAGE or tricine-SDS-PAGE.

Conclusions:

Partial digestion in solution followed by SDS-PAGE is an effective strategy for protein peptide mapping.
This approach facilitates the identification of larger peptide fragments, improving analytical outcomes.