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Heparinase I acts on a synthetic heparin pentasaccharide corresponding to the antithrombin III binding site

✍ Scribed by Guangli Yu; Laurie LeBrun; Nur Sibel Gunay; Debra Hoppensteadt; Jeanine M Walenga; Jawed Fareed; Robert J Linhardt

Book ID
117256912
Publisher
Elsevier Science
Year
2000
Tongue
English
Weight
174 KB
Volume
100
Category
Article
ISSN
0049-3848

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1H NMR and 13C NMR relaxation measurements at different magnetic field strengths were used to study the nature of overall and internal motions, in aqueous solution, of the synthetic pentasaccharide (A-G-A\*-I-A M) corresponding to the binding site of heparin for antithrombin III. Two-dimensional dou

Examination, by 1H-n.m.r. spectroscopy,
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 πŸ“‚ Article πŸ“… 1989 πŸ› Elsevier Science 🌐 English βš– 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