Titlebook: Heparin and Related Polysaccharides; David A. Lane,Ingemar Bj?rk,Ulf Lindahl Book 1992 The Editor(s) (if applicable) and The Author(s), un

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Chemical Synthesis and Hemisynthesis in the Field of Glycosaminoglycansd secondary hydroxyls. The biological function of these glycosaminoglycans is at least in part related to precise distributions of these functional groups on unique oligosaccharide sequences as illustrated by the binding of heparin to antithrombin III which involves a unique pentasaccharide sequence

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Structural Analysis of Periodate-Oxidized Heparin. The GlcNSO. residues at the sites of cleavage are converted into anhydromannose (AMan) residues. Reduction of heparin cleavage products with NaB.H. yields mixtures of di- and tetrasaccharides with reducing terminal [.H]anhydromannitol residues. The identification and quantification of these oligos

HAUNT

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Regulation of the Gene that Encodes the Peptide Core of Heparin Proteoglycan and Other Proteoglycansough the neutral trisaccharide, Gal?l→3Gal?l→4Xyl?→Ser (for review, see Rodén, 1980). The heparin/heparan sulfate family of glycosaminoglycans is formed in the Golgi by the sequential addition of alternating GlcA and GlcNAc onto this trisaccharide, whereas the chondroitin sulfate family of glycosami

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ADORE

Syndecan — A Cell Surface Proteoglycan that Selectively Binds Extracellular Effector Molecules proteoglycan containing both heparan sulfate and chondroitin sulfate glycosaminoglycan (GAG) chains (Rapraeger et al., 1985). The ratio and total amount of GAG bound to syndecan is known to vary in different tissues (Sanderson & Bernfield, 1988; Salmivirta et al., 1991) and cells (Rapraeger 1989).

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