Abstract
Current diagnostic methods using serum proteins are often insensitive, non-specific and lack the ability to predict the future outcome of treatment. With the exception of albumin and C-reactive protein, most serum proteins are glycosylated. Carbohydrate structures on serum proteins are very complex and for any particular protein, there coexists in the blood the same molecule with different carbohydrate structures (glycoforms). These reflect the sources of the molecule, and the particular physiological and biochemical conditions that existed when the molecule was synthesised and released. When disease is present, the glycoform distribution changes according to the type of disease and particular protein studied. Over one hundred proteins have been identified in the blood. The carbohydrate changes on these molecules, therefore, provide a wealth of untapped diagnostic information. For reviews of glycosylation changes in disease the reader should consult previous literature1–3.
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References
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Turner, G.A., Goodarzi, M.T. (1998). Oligosaccharide Profiling of Acute-Phase Proteins: A Possible Strategy Towards Better Markers in Disease. In: Axford, J.S. (eds) Glycoimmunology 2. Advances in Experimental Medicine and Biology, vol 435. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5383-0_18
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DOI: https://doi.org/10.1007/978-1-4615-5383-0_18
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