Abstract
The epidermal growth factor receptor is a membrane glycoprotein expressed in a large variety of higher eukaryotic cells. Its role in growth and development as well as its high levels of expression in certain types of cancer have stimulated wide-ranging studies at the tissue, cell, and molecular levels. The receptor is a 175-kDa single polypeptide protein consisting of an extracellular EGF binding domain, a transmembrane peptide, and an intracellular protein tyrosine kinase domain (1,2). The extracellular domain contains 12 potential glycosylation sites and is heavily glycosylated (3–5). The structures of some of these carbohydrate antigens have been identified by either determining the specificity of monoclonal antibodies raised against the receptor or, conversely, by investigating the reactivity of unrelated monoclonals of known antigenic specificity with purified receptor (6,7).
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© 1993 Humana Press Inc., Totowa, NJ
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Gregoriou, M. (1993). Purification of the EGF Receptor for Oligosaccharide Studies. In: Hounsell, E.F. (eds) Glycoprotein Analysis in Biomedicine. Methods in Molecular Biology, vol 14. Humana Press. https://doi.org/10.1385/0-89603-226-4:189
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DOI: https://doi.org/10.1385/0-89603-226-4:189
Publisher Name: Humana Press
Print ISBN: 978-0-89603-226-2
Online ISBN: 978-1-59259-501-3
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