Abstract
Heparin was linked covalently to Sepharose by a reaction between a uronic acid-carboxyl group of heparin and aminohexyl-Sepharose. The characteristics of this material in binding thrombin and antithrombin-heparin cofactor, was compared with those of heparin-aminoethylbromide method (heparin-Sepharose I). Although all the preparations bind thrombin and antithrombin-heparin cofactor they differ in their binding properties and purification efficiency. Highly purified antithrombin heparin cofactor was isolated by adsorption on heparinaminohexylsepharose and desorption with 1.0 M NaCl. The greatest purification of thrombin is obtained by absorption on heparin-Sepharose I and successive elution with 0.3 M and 0.4 M NaCl. Heparin-Sepharose prepared from partially degraded heparin has a relatively low affinity for thrombin and antithrombin-heparin cofactor.
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