Structural variation in the antithrombin III binding site region and its occurrence in heparin from different sources

A tetrasaccharide possessing a biosynthetically permissible structural variability in and adjacent to the antithrombin III (ATIII) binding site has been isolated from heparin lyase depolymerized bovine lung heparin by using strong anion-exchange high-pressure liquid chromatography (SAX-HPLC). On the...

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Veröffentlicht in:	Biochemistry (Easton) 1990-05, Vol.29 (18), p.4362-4368
Hauptverfasser:	Loganathan, Duraikkannu, Wang, Hui M, Mallis, Larry M, Linhardt, Robert J
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Antithrombin III - metabolism Binding Sites Carbohydrate Conformation Carbohydrate Sequence Cattle heparin Heparin - metabolism Heparin Lyase Magnetic Resonance Spectroscopy Molecular Sequence Data Polysaccharide-Lyases Sheep Structure-Activity Relationship Swine
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