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Purification of Glycoproteins and Their Use as Immunogens

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Book cover Immunochemical Protocols

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 80))

Abstract

Glycosylation is a major posttranslational modification that produces heterogeneity in a protein and results in a group of structurally different species called glycoforms. Protein-associated oligosaccharides are large, structurally diverse molecules, and the biological roles ascribed to them are numerous. Some of these functions include the following: intercellular adhesion, adhesion of microorganisms, including viruses to target cells, and modulation of immunological activity of polypeptide chains.

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References

  1. O’Shannessy, D J., Voorstad, P. J., and Quarles, R. H. (1987) Quantitation of glycoproteins on electroblots using the biotin-streptavidin complex. Anal Biochem. 163, 204–209.

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  2. Haselbeck, A. and Hosel, W. (1990) Description and application of an immunological detection system for analyzing glycoproteins on blots. Glycoconjugate J. 7, 63–74.

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© 1998 Humana Press Inc., Totowa, NJ

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Szewczyk, B., Summers, D.F. (1998). Purification of Glycoproteins and Their Use as Immunogens. In: Pound, J.D. (eds) Immunochemical Protocols. Methods in Molecular Biology™, vol 80. Humana Press. https://doi.org/10.1007/978-1-59259-257-9_9

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  • DOI: https://doi.org/10.1007/978-1-59259-257-9_9

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-493-8

  • Online ISBN: 978-1-59259-257-9

  • eBook Packages: Springer Protocols

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