Published February 15, 1984
| Published
Journal Article
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Biologic activity in a fragment of recombinant human interferon α
Chicago
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Abstract
To attempt to locate functionally important regions of the interferon (IFN) molecule, recombinant human IFN-α2 was subjected to proteolytic digestion. The bacterial proteinase thermolysin produced two major complementary fragments, HuIFN-α2-(1-110) and HuIFN-α2-(111-153). After reduction with 2-mercaptoethanol and separation of the two major fragments on NaDodSO4/polyacrylamide gel electrophoresis, antiviral activity persisted in the larger, Mr 12,000, fragment consisting of the amino-terminal 110 amino acids.
Additional Information
© 1984 by the National Academy of Sciences. Communicated by Christian B. Anfinsen, November 2, 1983. We thank Dr. N.-Y. Nguyen for amino acid analysis and Dr. R. Wetzel for helpful discussion. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.Attached Files
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Additional details
- PMCID
- PMC344760
- Eprint ID
- 8086
- Resolver ID
- CaltechAUTHORS:ACKpnas84
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