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Human leukocyte interferon: relationship between molecular structure and species specificity
Summary
Human leukocyte interferon separates into two types based on polynucleotide binding. One type, with polynucleotide affinity, is likely native, while the altered type shows increased bovine cell activity.
Area of Science:
- Immunology
- Biochemistry
- Molecular Biology
Background:
- Human leukocyte interferon exhibits heterogeneity.
- Previous studies suggest different interferon subspecies exist.
Purpose of the Study:
- To investigate the separation and characteristics of human leukocyte interferon subspecies.
- To explore the relationship between polynucleotide binding and interferon properties.
Main Methods:
- Polynucleotide-agarose affinity chromatography was used to separate interferon subspecies.
- Sodium dodecyl sulfate/polyacrylamide gel electrophoresis (SDS-PAGE) analyzed molecular weights.
Main Results:
- Two distinct interferon classes were identified: one with polynucleotide-binding (21 kDa) and one without (13.5-15 kDa).
- Loss of polynucleotide affinity correlated with a degradative alteration and increased heterospecific activity on bovine cells.
- The modified interferon retained antiviral activity.
Conclusions:
- Polynucleotide-agarose chromatography is effective for human leukocyte interferon purification.
- Interferon alteration affects species specificity, possibly linked to the polynucleotide binding site.
- Separation facilitates rational purification and preparation of homogeneous interferon subspecies.