Structural characterization of low molecular weight heparins.
Low molecular weight heparins (LMWHs) obtained by different depolymerization processes can be distinguished from each other by characteristic end-residues, which are easily identified and quantified by nuclear-magnetic-resonance (NMR) spectroscopy. NMR spectroscopy characterizes major sulfation patterns as well as minor sequences such as the antithrombin-binding sequence and the linkage region of LMWHs. Artifacts associated with base-induced modifications such as the formation of iduronic acid epoxide and aziridine derivatives of N-sulfoglucosamine residues can also be detected. The influence of these modifications on the binding of heparins and LMWHs to proteins other than antithrombin are discussed.
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G. Ronzoni Institute for Chemical and Biochemical Research, Milan, Italy.
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D000818:Animals; D001665:Binding Sites; D004187:Disaccharides / Q000737:chemistry; D006495:Heparin, Low-Molecular-Weight / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure
D004187:Disaccharides; D006495:Heparin, Low-Molecular-Weight