A qualitative and quantitative analysis of von Willebrand factor contained in a very high-purity plasma-derived FVIII concentrate
Article first published online: 13 JAN 2012
© 2012 The Author(s). Vox Sanguinis © 2012 International Society of Blood Transfusion
Volume 103, Issue 1, pages 35–41, July 2012
How to Cite
Samor, B., Michalski, C., Brandin, M.-P., Andre, M.-H., Chtourou, S. and Tellier, Z. (2012), A qualitative and quantitative analysis of von Willebrand factor contained in a very high-purity plasma-derived FVIII concentrate. Vox Sanguinis, 103: 35–41. doi: 10.1111/j.1423-0410.2011.01576.x
- Issue published online: 12 JUN 2012
- Article first published online: 13 JAN 2012
- Received: 17 December 2010, revised 28 October 2011, accepted 2 November 2011
- FVIII immunogenicity;
- haemophilia A;
- very high-purity FVIII;
- von Willebrand factor
Background and Objectives We studied the structural and functional properties of von Willebrand factor (VWF) molecules present in a very high-purity plasma-derived factor VIII concentrate (VHP pdFVIII – Factane®) because several observations suggest that the presence of VWF in factor VIII (FVIII) preparations may decrease their immunogenicity.
Materials and Methods Ten marketed batches of VHP pdFVIII (Factane®) with levels of VWF ranging from 15 to 39 IU/100 IU FVIII were analysed. The VWF multimeric pattern was studied by agarose gel electrophoresis. The binding of VWF to FVIII was studied by gel filtration and ELISA. The binding of VWF to GPIb was analysed by ELISA.
Results The results showed that high-molecular-weight multimers of VWF were present in VHP pdFVIII (Factane®). VWF subunits maintain a triplet structure similar to that of normal plasma. Regardless of the VWF content, all FVIII molecules of each batch were co-eluted with VWF, and no free FVIII was detectable. By immunoassays, VWF was found to be able to bind to FVIII and platelet GPIb in a similar manner to that of VWF in normal plasma.
Conclusions In all the VHP pdFVIII (Factane®) batches studied, regardless of the level of VWF, the structure and capacity of VWF binding to FVIII and to platelet GPIb were fully preserved.