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Total synthesis of a heparin pentasaccharide fragment having high affinity for antithrombin III

✍ Scribed by Pierre Sinaÿ; Jean-Claude Jacquinet; Maurice Petitou; Philippe Duchaussoy; Isidore Lederman; Jean Choay; Giangiacomo Torri

Book ID
102641180
Publisher
Elsevier Science
Year
1984
Tongue
English
Weight
254 KB
Volume
132
Category
Article
ISSN
0008-6215

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✦ Synopsis

Heparin is a sulfated glucosaminoglycan with a well-known anticoagulant activity' , and the active molecules have a high affinity for antithrombin III (AT-III), thereby enhancing the effects of this inhibitor on procoagulant proteases. The structures of highaffinity oligosaccharides, prepared from heparin by extraction, partial deaminative cleavage, or partial depolymerisation with bacterial heparinase, have been studied2. This work led to the hypothesis3 that the minimum sequence that binds to AT-III was contained in the pentasaccharide 1. H

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Examination, by 1H-n.m.r. spectroscopy, of the binding of a synthetic, high-affinity heparin pentasaccharide to human antithrombin III
✍ Peter Gettins; Jean Choay 📂 Article 📅 1989 🏛 Elsevier Science 🌐 English ⚖ 519 KB

Binding of a synthetic, high-affinity heparin pentasaccharide and of intact heparin to both native and elastase-modified human antithrombin III have been examined by 'H-n.m.r. spectroscopy. The pentasaccharide perturbs many protein resonances in the same way as does intact heparin. There are, howeve