Figure 2
PolyP-induced changes in fibrin formation and structure. (A) Fibrinogen (2.4μM) was clotted in the absence (gray line) and presence (black line) of polyP65 (325μM) by an activation mix of thrombin (0.25 U/mL) and CaCl2 (5mM). The turbidity was monitored at 340 nm every 12 seconds for 30 minutes, and the results are expressed as mean ± SEM (n = 4). (B) Fibrinopeptide release from fibrinogen during polymerization with thrombin (0.2 U/mL) and CaCl2 (5mM) was monitored over time by reverse-phase high-performance liquid chromatography (HPLC) in the absence (open symbols) and presence (closed symbols) of polyP65 (325μM). The concentration of fibrinopeptide A (circles) and fibrinopeptide B (triangles) at each time point is expressed as a fraction of maximal release ([FP]/[FP]max, so that complete release is equal to 1). The inset shows the linear part of the curve.

PolyP-induced changes in fibrin formation and structure. (A) Fibrinogen (2.4μM) was clotted in the absence (gray line) and presence (black line) of polyP65 (325μM) by an activation mix of thrombin (0.25 U/mL) and CaCl2 (5mM). The turbidity was monitored at 340 nm every 12 seconds for 30 minutes, and the results are expressed as mean ± SEM (n = 4). (B) Fibrinopeptide release from fibrinogen during polymerization with thrombin (0.2 U/mL) and CaCl2 (5mM) was monitored over time by reverse-phase high-performance liquid chromatography (HPLC) in the absence (open symbols) and presence (closed symbols) of polyP65 (325μM). The concentration of fibrinopeptide A (circles) and fibrinopeptide B (triangles) at each time point is expressed as a fraction of maximal release ([FP]/[FP]max, so that complete release is equal to 1). The inset shows the linear part of the curve.

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