Purification of antithrombin ‘Vicenza’: a molecule with normal heparin affinity and impaired reactivity to thrombin
- 1 February 1985
- journal article
- research article
- Published by Wiley in British Journal of Haematology
- Vol. 59 (2), 259-263
- https://doi.org/10.1111/j.1365-2141.1985.tb02992.x
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.This publication has 17 references indexed in Scilit:
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