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SDS-Polyacrylamide Gel Electrophoresis of Peptides

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Book cover The Protein Protocols Handbook

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Abstract

Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) has proven to be among the most useful tools yet developed in the area of molecular biology. The discontinuous buffer system, first described by Laemmli (1), has made it possible to separate, visualize, and compare readily the component parts of complex mixtures of molecules (e.g., tissues, cells). SDS-PAGE separation of proteins and peptides makes it possible to quantify the amount of a particular protein/peptide in a sample, obtain fairly reliable molecular mass information, and, by combining SDS-PAGE with immunoelectroblotting, evaluate the antigenicity of proteins and peptides. SDS-PAGE is both a powerful separation system and a reliable preparative purification technique (2 and see Chapter 11).

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References

  1. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–695.

    Article  PubMed  CAS  Google Scholar 

  2. Judd, R. C. (1988) Purification of outer membrane proteins of the Gram negative bacterium Neisseria gonorrhoeae. Anal. Biochem. 173, 307–316.

    Article  PubMed  CAS  Google Scholar 

  3. Dreyfuss, G., Adam, S. A., and Choi, Y. D. (1984) Physical change in cytoplasmic messenger ribonucleoproteins in cells treated with inhibitors of mRNA transcription. Mol. Cell. Biol. 4, 415–423.

    PubMed  CAS  Google Scholar 

  4. Schagger, H. and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368–397.

    Article  PubMed  CAS  Google Scholar 

  5. Judd, R. C. (1986) Evidence for N-terminal exposure of the PIA subclass of protein I of Neisseria gonorrhoeae. Infect. Immunol. 54, 408–414.

    CAS  Google Scholar 

  6. Moos, M., Jr. and Nguyen, N. Y. (1988) Reproducible high-yield sequencing of proteins electrophoretically separated and transferred to an inert support. J. Biol. Chem. 263, 6005–6008.

    PubMed  CAS  Google Scholar 

  7. Stoll, V. S. and Blanchard, J. S. (1990) Buffers: principles and practice, in Methods in Enzymology, vol. 182, A Guide to Protein Purification (Deutscher, M. P., ed.), Academic, San Diego, CA, pp. 24–38.

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© 1996 Humana Press Inc., Totowa, NJ

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Judd, R.C. (1996). SDS-Polyacrylamide Gel Electrophoresis of Peptides. In: Walker, J.M. (eds) The Protein Protocols Handbook. Springer Protocols Handbooks. Humana Press. https://doi.org/10.1007/978-1-60327-259-9_16

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  • DOI: https://doi.org/10.1007/978-1-60327-259-9_16

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-338-2

  • Online ISBN: 978-1-60327-259-9

  • eBook Packages: Springer Book Archive

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