GLYCOPROTEIN

glīˌkōprōˈtēn, organic compound composed of both a protein and a carbohydrate joined together in covalent chemical linkage. These structures occur in many life forms; they are prevalent and important in mammalian tissues. The attached carbohydrate may have several effects: it may help the protein to fold in the proper geometry, stabilize the protein, affect physical properties such as solubility or viscosity, helps it to orient correctly in a membrane, or make it recognizable to another biochemical or cell (see immunity). Many proteins released by cells to the blood and other fluids are glycoproteins. One set of glycoproteins also carry the blood group determinants. The carbohydrate portion of a glycoprotein is usually a small sugar or no more than 8 to 10 individual monosaccharide units. Combinations of up to seven of the many different sugar molecules known to occur in nature comprise the saccharide portions of mammalian glycoproteins: glucose, glucosamine, galactose, galactosamine, mannose, fucose, and sialic acid (a derivative of glucosamine). The linkage between the oligosaccharide and the protein occurs by formation of a chemical bond to only one of four protein amino acids: asparagine, hydroxylysine, serine, or threonine. Solutions of glycoproteins usually exhibit high viscosity, an observation explaining the highly viscous character of egg white, which is composed largely of the glycoprotein ovalbumin. Salivary mucus contains the glycoprotein called mucin. Among other glycoproteins, one particularly interesting example is isolated from certain antarctic fishes who survive near-freezing water temperatures as a result of freezing-point depression of their blood serum by a globular glycoprotein. This molecule is a remarkably effective freezing point depressant.

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