Figure 2.
Figure 2. Force distribution histograms of fibrinogen binding to purified surface-bound αIIbβ3 preincubated with Ca2+ or Mn2+. In the experiments shown, fibrinogen-coated beads were oscillated at 5 Hz touching the αIIbβ3-coated pedestals repeatedly. These data represent rupture forces greater than 60 pN, indicative of specific fibrinogen binding to αIIbβ3.18 The average yield strength in pN and the cumulative probability of specific fibrinogen binding (%) for each histogram are also shown. (A) Fibrinogen binding to αIIbβ3 immobilized in the presence of 1 mM Ca2+. (B) Fibrinogen binding to αIIbβ3 immobilized in the presence of 1 mM Mn2+. (C) Fibrinogen binding to αIIbβ3 treated with 1 mM Mn2+ measured in the presence of 50 μM tirofiban. (D) Fibrinogen binding to αIIbβ3 treated with 1 mM Mn2+ measured in the presence of 100 μg/mL abciximab.

Force distribution histograms of fibrinogen binding to purified surface-bound αIIbβ3 preincubated with Ca2+ or Mn2+. In the experiments shown, fibrinogen-coated beads were oscillated at 5 Hz touching the αIIbβ3-coated pedestals repeatedly. These data represent rupture forces greater than 60 pN, indicative of specific fibrinogen binding to αIIbβ3.18  The average yield strength in pN and the cumulative probability of specific fibrinogen binding (%) for each histogram are also shown. (A) Fibrinogen binding to αIIbβ3 immobilized in the presence of 1 mM Ca2+. (B) Fibrinogen binding to αIIbβ3 immobilized in the presence of 1 mM Mn2+. (C) Fibrinogen binding to αIIbβ3 treated with 1 mM Mn2+ measured in the presence of 50 μM tirofiban. (D) Fibrinogen binding to αIIbβ3 treated with 1 mM Mn2+ measured in the presence of 100 μg/mL abciximab.

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