| Literature DB >> 2083874 |
B Casu1.
Abstract
Heparins used in therapy are largely constituted by sequences of the trisulfated disaccharide L-iduronic acid-2-sulfate----D-glucosamine-N,6-disulfate. These regular sequences are interrupted by undersulfated (occasionally, oversulfated) sequences containing D-glucuronic acid and N-acetylated D-glucosamine. Different heparin sequences are binding domains for heparin cofactors and plasma proteins. The active site for antithrombin is a specific pentasaccharide sequence containing 3-O-sulfated D-glucosamine. Heparin cofactor-II binds, less specifically, mostly to the regular sequences. The conformational flexibility of iduronic acid residues contributes to the binding versatility and to the 'biological reactivity' of heparin.Entities:
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Year: 1990 PMID: 2083874 DOI: 10.1159/000216162
Source DB: PubMed Journal: Haemostasis ISSN: 0301-0147