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Staining of Glycoproteins/Proteoglycans on SDS-Gels

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The Protein Protocols Handbook

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Abstract

Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) is a commonly employed technique for separation of proteins according to size. Among other applications, it is used for identification and characterization of proteins on the basis of molecular weight determinations. In this chapter, staining methods will be described that permit detection of highly glycosylated proteins on SDS gels at levels of a few nanograms.

Proteins with limited glycosylation are most often stained with Coomassie brilliant blue or, if high sensitivity is needed, with a silver-stain (1). These stains, however, are far less sensitive when used for detecetion of highly glycosylated proteoglycans (protein-glycosaminoglycans) or glycoproteins (protein-oligosaccharides), leading to weak staining or even failure of detection. This is presumably the result of steric interference by the carbohydrates with the binding of silver ions.

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Møller, H.J., Poulsen, J.H. (2009). Staining of Glycoproteins/Proteoglycans on SDS-Gels. In: Walker, J.M. (eds) The Protein Protocols Handbook. Springer Protocols Handbooks. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-59745-198-7_52

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  • DOI: https://doi.org/10.1007/978-1-59745-198-7_52

  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-60327-474-6

  • Online ISBN: 978-1-59745-198-7

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