Purification of antithrombin 'Vicenza': a molecule with normal heparin affinity and impaired reactivity to thrombin.
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.
D000990:Antithrombin III / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D006493:Heparin; D006801:Humans; D007123:Immunoelectrophoresis, Two-Dimensional; D013917:Thrombin / Q000494:pharmacology
C038873:antithrombin III Vicenza; D000990:Antithrombin III; D006493:Heparin; D013917:Thrombin