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Oversulfated chondroitin sulfate is a contaminant in heparin associated with adverse clinical events
Through detailed structural analysis, the contaminant was found to contain a disaccharide repeat unit of glucuronic acid linked β1→3 to a β-N-acetylgalactosamine, indicative of an allergic-type reaction.
Modulation of the Heparanase-inhibiting Activity of Heparin through Selective Desulfation, Graded N-Acetylation, and Glycol Splitting*
The combination of high inhibition of heparanase and low release/potentiation of ECM-bound growth factor indicates that N-acetylated, glycol-split heparins are potential antiangiogenic and antimetastatic agents that are more effective than their counterparts with unmodified backbones.
SST0001, a Chemically Modified Heparin, Inhibits Myeloma Growth and Angiogenesis via Disruption of the Heparanase/Syndecan-1 Axis
These results provide mechanistic insight into the antitumor action of SST0001 and validate its use as a novel therapeutic tool for treating multiple myeloma.
Conformer populations of L-iduronic acid residues in glycosaminoglycan sequences.
Structural differences between non-wood plant celluloses: evidence from solid state NMR, vibrational spectroscopy and X-ray diffractometry
Combined quantitative (1)H and (13)C nuclear magnetic resonance spectroscopy for characterization of heparin preparations.
The sulfation patterns of pig and bovine mucosal commercial heparin preparations can be characterized and distinguished from each other easily by analysis of their monodimensional proton and carbon…
Structural features of low-molecular-weight heparins affecting their affinity to antithrombin.
Enoxaparin is consistently richer in shorter oligosaccharides than Tinzaparin and Dalteparin, and this study is critical for establishing correlations between structural features of LMWHs and their AT-mediated anticoagulant activity.
Alkaline N-deacetylation of chitin enhanced by flash treatments. Reaction kinetics and structure modifications
1H and 13C NMR spectral assignments of the major sequences of twelve systematically modified heparin derivatives.
Conformation of heparin pentasaccharide bound to antithrombin III.
- M. Hricovíni, M. Guerrini, A. Bisio, G. Torri, M. Petitou, B. Casu
- Chemistry, BiologyThe Biochemical journal
- 15 October 2001
An analysis of the three-dimensional structures of the pentasaccharide in the free state, and in the complex, revealed the binding to be accompanied by dihedral angle variation at the A-G and I-A(M) glycosidic linkages.