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Updated: Jun 1, 2026

Measurement of Factor V Activity in Human Plasma Using a Microplate Coagulation Assay
Published on: September 9, 2012
Allosteric activation of coagulation factor VIIa
Egon Persson1, Ole Hvilsted Olsen
1Haemostasis Biochemistry, Novo Nordisk A/S, Novo Nordisk Park, DK-2760 Maaloev, Denmark. egpe@novonordisk.com
Coagulation factor VIIa (FVIIa) initiates blood clotting upon binding its cofactor, tissue factor (TF). TF binding localizes clotting to injury sites and activates FVIIa, ensuring safe and effective thrombin generation.
Area of Science:
- Biochemistry
- Hematology
- Molecular Biology
Background:
- Coagulation factor VIIa (FVIIa) circulates at low concentrations, comprising a small fraction of total FVII.
- FVIIa initiates blood clotting upon encountering tissue factor (TF), exposed during vascular injury.
Purpose of the Study:
- To review the structure, function, and TF dependence of FVIIa.
- To elucidate the allosteric mechanism by which TF induces FVIIa activation.
Main Methods:
- Literature review of accumulated knowledge on FVIIa and TF.
- Analysis of structural and functional data to propose an allosteric mechanism.
Main Results:
- TF acts as a crucial safety mechanism by localizing clotting to injury sites.
- TF binding induces the maturation of zymogen-like FVIIa into its active cofactor-bound form.
- A plausible allosteric mechanism for TF-induced FVIIa activation is proposed.
Conclusions:
- TF is essential for the timely and localized initiation of blood coagulation.
- TF binding is critical for converting free FVIIa to its active conformation.
- Understanding this mechanism enhances knowledge of hemostasis and thrombosis.
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