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. Author manuscript; available in PMC: 2017 Nov 9.
Published in final edited form as: Semin Thromb Hemost. 2016 Apr 7;42(4):445–454. doi: 10.1055/s-0036-1571343

Figure 2. Contributions of FXIIIa to clot biochemical and mechanical stability.

Figure 2

FXIIIa crosslinking of plasma proteins [i.e. α2-antiplasmin, (α2-AP)] increases the resistance of the clot to fibrinolysis. Crosslinking of the fibrin α- (purple) and γ-chains (green) stiffens fibrin fibers and increases the mechanical stability of the clot. Increased mechanical stability renders the clot more resistant to shear forces. α-chain crosslinking enables RBC retention during clot contraction.39