Interactions between glycosaminoglycans and blood coagulation factors: 1. Affinity chromatography of glycosaminoglycans on thrombin-substituted agarose |
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Authors: | L.-Å. Fransson B. Havsmark |
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Affiliation: | Department of Physiological Chemistry 2, University of Lund, S-220 07 Lund, Sweden |
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Abstract: | Various glycosaminoglycans have been subjected to affinity chromatography on immobilized bovine thrombin. Chondroitin sulphate, dermatan sulphate and heparan sulphate variants with a sulphate-to-hexosamine molar ratio of ~ 1 exhibited weak affinities. Heparan sulphate/heparin fractions of higher sulphate content could be separated into material with high and low affinity for thrombin. Removal of N-sulphate followed by N-acetylation did not affect binding, whereas oxidation and cleavage of non-sulphated hexuronate abolished the interaction. Heparan-related molecules of high thrombin-affinity comprised sequences where large blocks of sulphated iduronate-containing repeats were joined via a few repeats carrying non-sulphated iduronate or glucuronate to form continuous segments that were larger than decasaccharide. |
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Keywords: | Polysaccharides heparin heparan sulphate thrombin antithrombin iduronic acid-sulphate GlcNAc 2-acetamido OseA hexuronic acid GlcA IdoA ester sulphate |
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