Abstract
Proteins with covalently bound sugars are known as glycoproteins and are widely distributed in nature, e.g., plants, animals, bacteria, and viruses. Hormones, enzymes, and toxins are examples of proteins that are both biologically active and glycosylated. In addition, a number of proteins on the cell’s surface, in cytosol, and in nucleus are glycosylated. During the last few years, enormous advances have been made in the understanding of glycoproteins, specifically their structure and biochemistry. This increased understanding is primarily due to the advent of new tools for the study of complex carbohydrates. These new analytical methods have allowed for the reporting of a large number of well-characterized glycoproteins. The complete analysis of a glycoprotein provides information on the primary structure of the oligosaccharides as well as their variation at individual glycosylation sites. Such analysis requires a multipronged approach involving mapping and characterization of oligosaccharides, which is described in Chapter 9 of this book, and determination of carbohydrate composition.
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Saddic, G.N., Ebert, M.B., Dhume, S.T., Anumula, K.R. (2002). Carbohydrate Composition Analysis of Glycoproteins Using Highly Sensitive Fluorescence Detection Methods. In: Kannicht, C. (eds) Posttranslational Modifications of Proteins. Methods in Molecular Biology™, vol 194. Humana Press. https://doi.org/10.1385/1-59259-181-7:023
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DOI: https://doi.org/10.1385/1-59259-181-7:023
Publisher Name: Humana Press
Print ISBN: 978-0-89603-678-9
Online ISBN: 978-1-59259-181-7
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