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.
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References
Deyl, Z. (1979) Electrophoresis. A survey of techniques and applications. Part A: Techniques. Elesevier, Amsterdam.
Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685.
Studier, F. W. (1973) Analysis of bacteriophage T7 early RNAs and proteins on slab gels. J. Mol. Biol. 79, 237–248.
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© 1984 Humana Press
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Smith, B.J. (1984). SDS Polyacrylamide Gel Electrophoresis of Proteins. In: Walker, J.M. (eds) Proteins. Methods in Molecular Biology™, vol 1. Humana Press. https://doi.org/10.1385/0-89603-062-8:41
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DOI: https://doi.org/10.1385/0-89603-062-8:41
Publisher Name: Humana Press
Print ISBN: 978-0-89603-062-6
Online ISBN: 978-1-59259-488-7
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