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Proteins pp 41-55 | Cite as

SDS Polyacrylamide Gel Electrophoresis of Proteins

  • B. J. Smith
Part of the Methods in Molecular Biology™ book series (MIMB, volume 1)

Abstract

Probably the most widely used of techniques for analyzing mixtures of proteins is SDS polyacrylamide gel electrophoresis. In this technique, proteins are reacted with the anionic detergent, sodium dodecylsulfate (SDS, or sodium lauryl sulfate) to form negatively charged complexes. The amount of SDS bound by a protein, and so the charge on the complex, is roughly proportional to its size. Commonly, about 1.4 g SDS is bound per 1 g protein, although there are exceptions to this rule. The proteins are generally denatured and solubilized by their binding of SDS, and the complex forms a prolate elipsoid or rod of a length roughly proportionate to the protein’s molecular weight. Thus, proteins of either acidic or basic pI form negatively charged complexes that can be separated on the bases of differences in charges and sizes by electrophoresis through a sieve-like matr ix of polyacrylamide gel.

Keywords

Sodium Lauryl Sulfate Ammonium Persulfate Acrylamide Content Acrylamide Monomer Reservoir Buffer 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

References

  1. 1.
    Deyl, Z. (1979) Electrophoresis. A survey of techniques and applications. Part A: Techniques. Elesevier, Amsterdam.Google Scholar
  2. 2.
    Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685.PubMedCrossRefGoogle Scholar
  3. 3.
    Studier, F. W. (1973) Analysis of bacteriophage T7 early RNAs and proteins on slab gels. J. Mol. Biol. 79, 237–248.PubMedCrossRefGoogle Scholar

Copyright information

© Humana Press 1984

Authors and Affiliations

  • B. J. Smith
    • 1
  1. 1.Institute of Cancer Research, Chester Beatty LaboratoriesRoyal Cancer HospitalLondonUK

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