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Purification and characterization of human leukocyte interferon components
The Journal of Biological Chemistry
|August 25, 1976
Summary
Human leukocyte interferon was purified using gel filtration and hydroxylapatite chromatography. This process yielded two distinct antiviral components, A and B, with different molecular weights but similar disulfide bond susceptibility.
Area of Science:
- Biochemistry
- Immunology
- Virology
Background:
- Human leukocyte interferon exhibits antiviral properties.
- Previous purification methods included acid ethanol extraction and affinity chromatography.
Purpose of the Study:
- To further purify human leukocyte interferon.
- To characterize the purified interferon components.
Main Methods:
- Gel filtration chromatography in the presence of sodium dodecyl sulfate.
- Hydroxylapatite adsorption chromatography.
- Isoelectric focusing and polyacrylamide gel electrophoresis.
Main Results:
- Interferon was purified to homogeneity with a molecular weight of 26,600.
- Two antiviral components, A and B, were resolved.
- Components A and B had apparent molecular weights of 20,000-16,000 and 16,000, respectively.
- Both components showed similar susceptibility to beta-mercaptoethanol reduction.
Conclusions:
- Human leukocyte interferon can be effectively purified using gel filtration and hydroxylapatite chromatography.
- The purified interferon consists of at least two distinct antiviral components.
- These components can be isolated with minimal loss of biological activity.