The Structural Characterization of Coagulation Factor IX/Factor X-Binding Protein Isolated from the Venom of Trimeresurus Flavoviridis
Inhibitor of the activation of prothrombin have been found in the venoms of Agkistrodon acutus (1) and Trimeresurus gramineus (2). The anticoagulant isolated from A. acutus inhibited the participation of factor Xa in the prothrombinase complex (3). Teng and Seegers have also reported that the activation of prothrombin was inhibited by a protein from A. acutus venom through its binding to factor Xa (4). We have developed a simple procedure of affinity chromatography on a column of insoluble factor X-Cellulofine to detect and concomitantly to isolate the factor X-binding protein from the venom of Deinagkistrodon acutus. We indicated that one of the anticoagulants in the venom of D. acutus is a factor X-binding protein.
KeywordsDisulfide Bridge Anticoagulant Protein Pancreatic Stone Protein Prothrombinase Complex Interchain Disulfide Bond
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