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. Author manuscript; available in PMC: 2010 Jan 1.

Published in final edited form as: Haemophilia. 2008 Aug 6;15(1):63–72. doi: 10.1111/j.1365-2516.2008.01826.x

Fig. 1 — (A) Binding stoichiometry between albumin-free full-length rFVIIIa (FVIII standard) and FIXa. Varying concentrations of FVIII were added to 1 nM FIXa and 20 μM PCPS, followed by the addition of 10 nM thrombin and 340 nM FX. The maximum rate of FXa generation was evaluated for each FVIII concentration and the stoichiometry was calculated using Scatchard transformation. (B) Titration of the 7^th International Standard (◆) and albumin-free rFVIII (■) in FVIII-deficient plasma in the APTT assay. (C) SDS-PAGE (a) and western blot (b) of FVIII standard. αFVIII-1 (B domain specific) and αFVIII-68 (light chain specific) were used as primary antibodies for b.

Fig. 1 — (A) Binding stoichiometry between albumin-free full-length rFVIIIa (FVIII standard) and FIXa. Varying concentrations of FVIII were added to 1 nM FIXa and 20 μM PCPS, followed by the addition of 10 nM thrombin and 340 nM FX. The maximum rate of FXa generation was evaluated for each FVIII concentration and the stoichiometry was calculated using Scatchard transformation. (B) Titration of the 7^th International Standard (◆) and albumin-free rFVIII (■) in FVIII-deficient plasma in the APTT assay. (C) SDS-PAGE (a) and western blot (b) of FVIII standard. αFVIII-1 (B domain specific) and αFVIII-68 (light chain specific) were used as primary antibodies for b.