Biochemical quality of the pharmaceutically licensed plasma OctaplasLG® after implementation of a novel prion protein (PrPSc) removal technology and reduction of the solvent/detergent (S/D) process time
Article first published online: 9 APR 2009
© 2009 The Author(s). Journal compilation © 2009 International Society of Blood Transfusion
Volume 97, Issue 3, pages 219–225, October 2009
How to Cite
Heger, A., Svae, T.-E., Neisser-Svae, A., Jordan, S., Behizad, M. and Römisch, J. (2009), Biochemical quality of the pharmaceutically licensed plasma OctaplasLG® after implementation of a novel prion protein (PrPSc) removal technology and reduction of the solvent/detergent (S/D) process time. Vox Sanguinis, 97: 219–225. doi: 10.1111/j.1423-0410.2009.01190.x
- Issue published online: 24 SEP 2009
- Article first published online: 9 APR 2009
- Received: 28 November 2008, revised 16 March 2009, accepted 17 March 2009, published online 9 April 2009
- biochemical characterization;
- plasma quality;
- affinity ligand chromatography;
Background and Objectives A new chromatographic step for the selective binding of pathological prion proteins (PrPSc) to an affinity ligand, developed and optimized for PrPSc capture and attached to synthetic resin particles (PRDT, USA; ProMetic BioSciences Ltd, Isle of Man, UK) was implemented into the manufacturing process of the solvent/detergent (S/D) treated biopharmaceutical quality plasma Octaplas®.
Materials and Methods Pilot batches of Octaplas® with the implemented chromatographic step [labelled as OctaplasLG® (ligand gel)] were manufactured by Octapharma PPGmbH, Vienna, Austria. The biochemical quality was compared directly after manufacturing as well as after 18 months storage. All samples were tested on global coagulation parameters, fibrinogen levels, activities of coagulation factors and protease inhibitors, ADAMTS13 levels, as well as markers of activated coagulation and fibrinolysis. In addition, von Willebrand factor multimeric analysis was performed.
Results The incorporation of this novel chromatography into the large-scale routine manufacturing process was shown to be technically feasible and the performance of the column was assessed to be excellent. The biochemical studies showed that Octaplas® and OctaplasLG® produced without and with the new column, respectively, demonstrate an identical biochemical quality. OctaplasLG® remained stable over a period of 18 months stored frozen. A parallel reduction of the S/D virus inactivation step from 4–4·5 to 1–1·5 h led to significantly higher activities of plasmin inhibitor.
Conclusion The studies confirmed that the affinity ligand chromatography under the developed conditions can be introduced into the Octaplas® manufacturing process, as a mean to reduce potentially present PrPSc, without hampering the proven quality of this product.