Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
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Characterization of Glycosaminoglycans by Capillary Electrophoresis, R.J. Linhardt, T. Toida, in Capillary Electrophoresis of Oligosaccharides and Complex Carbohydrates, S. Honda, P. Thibault, Eds. Humana Press, Totawa, NJ, 133-146, 2002.
Glycosaminoglycans are linear, sulfated polysaccharides that are found in virtually all animal tissues. With the exception of hyaluronic acid, glycosaminoglycans are biosynthesized as proteoglycans in which one or more glycosaminoglycan chains are attached to a core protein (1). Chondroitin and dermatan sulfates are comprised of alternating 1→3, 1→4 linked N-acetyl-D-galactosamine and hexuronic acid (either D-glucuronic or L-iduronic acid) residues. These saccharide residues can be O-sulfonated at various positions on both sugar residues. Heparin and heparan sulfate are structurally related and are comprised of a hexuronic acid residue (either L-iduronic or D-glucuronic acid) 1→4 linked to a D-glucosamine (either N-sulfo or N-acetyl-D-glucosamine) residue. Both saccharide residues can be O-sulfonated at a variety of different positions, making these glycosaminoglycans structurally complex. Hyaluronic acid contains a simple repeating structure of 1→3, 1→4 linked N-acetyl-D-glucosamine and D-glucuronic acid residues. Hyaluronic acid is an unusual glycosaminoglycan as it is not sulfonated and can have a very high molecular weight, up to 2 × 106 Da compared to 1–3 × 105 for the other glycosaminoglycans. Keratan sulfate is a glycosaminoglycan that contains no uronic acid and is comprised of a repeating 1→3, 1→4 linked, O-sulfonated N-acetyl-D-glu-cosamine and D-galactose residues.;
in Capillary Electrophoresis of Oligosaccharides and Complex Carbohydrates, S. Honda, P. Thibault, Eds. Humana Press, Totawa, NJ, 133-146; Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Methods in molecular biology (Clifton, N.J.); https://harc.rpi.edu/;