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Process-scale purification of immunoglobulin M concentrate
P K Ng1, P E O'Rourke, J D Andersen
1Pharmaceutical Division, Miles Inc., Berkeley, Calif 94701-1986.
Vox Sanguinis
|January 1, 1993
Summary
This study details a method for purifying Immunoglobulin M (IgM) concentrate, achieving 50% purity and 66% yield. The process includes solvent-detergent treatment for virus inactivation, ensuring product safety.
Area of Science:
- Biochemistry
- Immunology
- Process Chemistry
Background:
- Immunoglobulin M (IgM) is a crucial component of the adaptive immune system.
- Purification of IgM from plasma fractions is essential for therapeutic and research applications.
- Cohn fraction III is a source material for plasma protein purification.
Purpose of the Study:
- To develop and optimize a purification process for IgM concentrate.
- To ensure the safety of the IgM concentrate through virus inactivation.
- To characterize the efficiency and yield of the purification method.
Main Methods:
- Purification of IgM concentrate from Cohn fraction III.
- Optimization of euglobin precipitation using pH and ionic strength.
- Implementation of solvent-detergent treatment for viral inactivation.
- Assay of prekallikrein activator activity and C4a generating activity.
Main Results:
- The purification process achieved an overall yield of 66 +/- 8% and a concentrate purity of 50 +/- 5%.
- Euglobin precipitation efficiency was effectively controlled by pH and ionic strength.
- Prekallikrein activator activity in the final product was found to be insignificant.
- Solvent-detergent treatment was successfully integrated to inactivate lipid-enveloped viruses.
Conclusions:
- A robust and efficient method for IgM concentrate purification has been established.
- The implemented process ensures a high-purity IgM product with significant viral safety.
- Further studies are presented on controlling residual virucidal agents and C4a generation.