Purification of antithrombin ''Vicenza'': a molecule with normal heparin affinity and impaired reactivity to thrombin |
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| Authors: | G. Finazzi T. H. Tran T. Barbui F. Duckert |
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| Affiliation: | Divisione di Ematologia, Ospedali Riuniti, Bergamo, Italy;Coagulation and Fibrinolysis Laboratory, Kantonsspital Basle, Switzerland |
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| Abstract: | Antithrombin III (AT) 'Vicenza', a previously described dysfunctional AT associated with familial thrombosis, has been isolated by heparin affinity chromatography. The purified molecule has been investigated by SDS-polyacrylamide gel electrophoresis and crossed immunoelectrophoresis after incubation with different amounts of thrombin. A normal affinity for heparin has been demonstrated. However, evidence is produced that AT 'Vicenza' poorly inhibits thrombin. Present data suggest that AT 'Vicenza' consists of a population of two molecules, half of which does not form a complex with thrombin however and loses its heparin affinity upon thrombin treatment. |
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