Abstract
Prothrombin is the substrate of the prothrombinase which consists of factor Xa, factor Va, calcium ions and anionic phospholipid surfaces. A key question for understanding the prothrombinase complex is the molecular mechanism of the interaction of the vitamin K dependent proteins (factor Xa and prothrombin) with the extraordinary procoagulant phospholipid phosphatidylserine (PS). For this interaction a chelate model has been suggested: The calcium ions are thought to form a coordinate complex with the γ-carboxyglutamic acid (gla) residues of these vitamin K dependent proteins and the negatively charged headgroups of PS1,2.
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Hutterer, R., Hof, M. (1996). Binding of Prothrombin Fragment 1 to Phosphatidylserine Containing Vesicles: A Solvent Relaxation Study. In: Slavík, J. (eds) Fluorescence Microscopy and Fluorescent Probes. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1866-6_33
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DOI: https://doi.org/10.1007/978-1-4899-1866-6_33
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