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Purification of High Yield Extracellular Vesicle Preparations Away from Virus
Published on: September 12, 2019
A simple method for large-scale purification of plasma-derived apo-transferrin
Ester Ascione1, Livio Muscariello, Valentina Maiello
1Kedrion Research, S. Antimo, Napoli, 80029, Italy.
Biotechnology and Applied Biochemistry
|October 7, 2010
Summary
This study optimized a scalable purification process for pharmaceutical-grade apotransferrin (apo-Tf) from a waste product. The efficient method yields high-purity apo-Tf with preserved biological functions.
Area of Science:
- Biochemistry
- Protein Purification
- Pharmaceutical Manufacturing
Background:
- Apotransferrin (apo-Tf) is crucial for iron transport.
- Existing purification methods may not be scalable or preserve biological functions.
- Waste streams from Cohn fractionation are a potential source for valuable proteins.
Purpose of the Study:
- To develop and optimize an industrial-scale purification process for pharmaceutical-grade apo-Tf.
- To ensure the preservation of apo-Tf's physiological properties and functions.
- To utilize a waste product from the Cohn fractionation process.
Main Methods:
- Apo-Tf was isolated from fraction IV subfractions 1 and 4 (fraction IV-1,4).
- A single chromatographic step was employed for purification.
- Two viral inactivation/removal steps were integrated into the process.
Main Results:
- Achieved 80% yield at laboratory scale and 90% yield in scale-up lots.
- Obtained a purity level higher than 95% for the final apo-Tf product.
- The purified apo-Tf retained iron- and receptor-binding activities and exhibited normal glycosylation.
Conclusions:
- The optimized single-step chromatographic process is efficient for producing commercial quantities of apo-Tf.
- The purification method successfully yields sterile, pharmaceutical-grade apo-Tf with preserved functionality.
- This approach offers a viable method for upcycling a Cohn fractionation waste product.
