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)


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.


Sodium Lauryl Sulfate Ammonium Persulfate Acrylamide Content Acrylamide Monomer Reservoir Buffer 
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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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