Biochemical characterization of bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI) |
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| Authors: | Zuzana Valnickova Morten Thaysen-Andersen Peter Højrup Trine Christensen Kristian W Sanggaard Torsten Kristensen Jan J Enghild |
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| Institution: | (1) From Center for Insoluble Protein Structures (inSPIN) and Interdisciplinary Nanoscience Center (iNANO), Department of Molecular Biology, Science Park, University of Aarhus, Gustav Wieds Vej 10c, 8000 Aarhus C, Denmark;(2) Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark |
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| Abstract: | Background TAFI is a plasma protein assumed to be an important link between coagulation and fibrinolysis. The three-dimensional crystal
structures of authentic mature bovine TAFI (TAFIa) in complex with tick carboxypeptidase inhibitor, authentic full lenght
bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI), and recombinant human TAFI have recently been solved. In
light of these recent advances, we have characterized authentic bovine TAFI biochemically and compared it to human TAFI. |
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