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- W1259806904 abstract "This chapter focuses on glycoproteins, which are a wide range of compounds of diverse structure and function, and are components of cell membranes, intercellular matrices, and extracellular fluids, such as plasma. They occur in soluble and membrane-bound forms. The proportion of carbohydrates varies considerably in glycoproteins derived from different tissues or from various sources. Glycoproteins containing high amounts of carbohydrate include glycophorin, a membrane constituent of human erythrocytes, and soluble blood group substances. In glycoproteins, the protein and the carbohydrate residues are bound in covalent linkage. The amino acid residue that participates in the N-glycosidic linkage is asparagine, and the amino acid residues that participate in O-glycosidic linkage are serine, threonine, hydroxylysine, and hydroxyproline. The glycoproteins exhibit microheterogeneity, which arises from incomplete synthesis or partial degradation and poses problems in the purification and characterization of glycoproteins. The monosaccharides are hexoses and their derivatives pentoses, and sialic acids derived from neuraminic acid, a nine-carbon sugar. The most common type of sialic acid is N-acetylneuraminic acid. In all glycoproteins, the polypeptide component is synthesized first on the membrane-bound ribosomes of the rough endoplasmic reticulum, and then the carbohydrate side chains are added during passage through the endoplasmic reticulum and Golgi apparatus. The carbohydrate additions involve specific glycosyltransferases and their substrates and, in some glycoproteins, an oligosaccharide carrier known as dolichol. Glycoproteins can also be formed by addition of carbohydrate residues without any of the complex enzymatic pathways of carbohydrate addition." @default.
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- W1259806904 date "2002-01-01" @default.
- W1259806904 modified "2023-10-01" @default.
- W1259806904 title "Heteropolysaccharides I: Glycoproteins and Glycolipids" @default.
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- W1259806904 doi "https://doi.org/10.1016/b978-012095440-7/50012-3" @default.
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