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A compound in which carbohydrate (sugar) is covalently linked to protein. The carbohydrate may be in the form of monosaccharides, disaccharides, oligosaccharides, or polysaccharides, and is sometimes referred to as glycan. The sugar may be linked to sulfate or phosphate groups. In different glycoproteins, 100–200 glycan units may be present. Therefore, the carbohydrate content of these compounds varies markedly, from 1% (as in the collagens), to 60% (in certain mucins), to >99% (in glycogen). See Collagen, Glycogen
Glycoproteins are ubiquitous in nature, although they are relatively rare in bacteria. They occur in cells, in both soluble and membrane-bound forms, as well as in the intercellular matrix and in extracellular fluids, and include numerous biologically active macromolecules. A number of glycoproteins are produced industrially by genetic engineering techniques for use as drugs; among them are erythropoietin, interferons, colony stimulating factors, and blood-clotting factors. See Genetic engineering
In most glycoproteins, the carbohydrate is linked to the polypeptide backbone by either N- or O-glycosidic bonds. A different kind of bond is found in glycoproteins that are anchored in cell membranes by a special carbohydrate-containing compound, glycosylphosphatidylinositol, which is attached to the C-terminal amino acid of the protein. A single glycoprotein may contain more than one type of carbohydrate-peptide linkage. N-linked units are typically found in plasma glycoproteins, in ovalbumin, in many enzymes (for example, the ribonucleases), and in immunoglobulins. O-linked units are found in mucins; collagens; and proteoglycans (typical constituents of connective tissues), including chondroitin sulfates, dermatan sulfate, and heparin. See Albumin, Carbohydrate, Enzyme, Immunoglobulin, Monosaccharide, Oligosaccharide, Polysaccharide, Protein
Within any organism, all molecules of a particular protein are identical. In contrast, a variety of structurally distinct carbohydrate units are found not only at different attachment sites of a glycoprotein but even at each single attachment site—a phenomenon known as microheterogeneity. For instance, ovalbumin contains one glycosylated amino acid, but over a dozen different oligosaccharides have been identified at that site, even in a preparation isolated from a single egg of a purebred hen.