Abstract
Glycoproteins are widely distributed in nature, not only in animal cells but also in plants, microorganisms and viruses. Structurally, glycoproteins can be distinguished from other proteins by the presence of sugars covalently linked to the polypeptide backbone. Thus, glycoproteins can be defined as macromolecules having a normal polypeptide backbone that is biosynthesized by the usual protein-synthesizing machinery, and to which carbohydrate moieties have been covalently attached by cotranslational or posttranslational events [1]. Glycoproteins occur in cells in both soluble and membrane-bound forms, and are also found in the intracellular matrix and the extracellular fluid. The intense interest in these molecules is due to the fact that they are involved in diverse biological functions including immunological protection, enzymatic catalysis, hormonal control and storage, blood clotting, ion transport, cell adhesion, molecular recognition, lubrication, structural support and many other functions [2]. A few well-known glycoproteins include immunoglobulins, gonadotropins, ribonucleases, thyroid stimulating hormone, thyroglobulin, antifreeze glycoprotein, mucous glycoproteins, fibronectin and collagen [3].
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Pan, Y.T., Elbein, A.D. (1990). Oligosaccharide chains of glycoproteins. In: Jucker, E. (eds) Progress in Drug Research / Fortschritte der Arzneimittelforschung / Progrès des recherches pharmaceutiques. Progress in Drug Research / Fortschritte der Arzneimittelforschung / Progrès des recherches pharmaceutiques, vol 34. Birkhäuser Basel. https://doi.org/10.1007/978-3-0348-7128-0_4
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