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Large scale purification of human fibroblast interferon
Preparative Biochemistry
|January 1, 1980
Summary
Human fibroblast interferon was purified 4,000-fold using a two-step chromatography method. This process achieved high specific activity and a good overall recovery of interferon, demonstrating an effective purification strategy.
Area of Science:
- Biochemistry
- Immunology
- Protein Purification
Background:
- Interferons are crucial signaling proteins in the immune system.
- Efficient purification of human fibroblast interferon is essential for research and therapeutic applications.
Purpose of the Study:
- To develop and optimize a partial purification protocol for human fibroblast interferon.
- To achieve a high level of specific activity and recovery of purified interferon.
Main Methods:
- Partial purification of human fibroblast interferon.
- Utilized a tandem chromatographic approach involving concanavalin A-agarose followed by phenyl-agarose columns.
Main Results:
- Achieved an approximate 4,000-fold purification of human fibroblast interferon.
- The purified interferon exhibited a specific activity of approximately 4 x 10(7) units/mg.
- An overall recovery of about 60% of the initial interferon activity was obtained.
Conclusions:
- The described two-step chromatographic method is effective for the partial purification of human fibroblast interferon.
- This protocol yields a highly active interferon preparation with substantial recovery, suitable for further studies.