American Society of Hematology

Fig. 7.

$Fig. 7. Inhibition of factor V des B activity by factor V C2 domain-affinity purified RS and H5 fractions. The Protein A Sepharose binding fraction from 0.5 mL RS plasma and 10 mL of unfractionated H5 plasma were applied to ≈1 mL of factor V C2 domain-Sepharose and serially eluted with glycine-HCl (elution step 1), triethylamine (elution step 2), and ethylene glycol (elution step 3), as described in Materials and Methods. A total of 10 ≈1-mL fractions after each buffer change were pooled, concentrated to a final volume of ≈0.5 mL, and then evaluated for inhibitory activity in the prothrombinase assay. Residual factor V activity is plotted against the individual elution steps for the RS (▧) and H5 (▨) fractions.$

Inhibition of factor V des B activity by factor V C2 domain-affinity purified RS and H5 fractions. The Protein A Sepharose binding fraction from 0.5 mL RS plasma and 10 mL of unfractionated H5 plasma were applied to ≈1 mL of factor V C2 domain-Sepharose and serially eluted with glycine-HCl (elution step 1), triethylamine (elution step 2), and ethylene glycol (elution step 3), as described in Materials and Methods. A total of 10 ≈1-mL fractions after each buffer change were pooled, concentrated to a final volume of ≈0.5 mL, and then evaluated for inhibitory activity in the prothrombinase assay. Residual factor V activity is plotted against the individual elution steps for the RS (▧) and H5 (▨) fractions.

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