Ackerman, Samuel K. and Zur Nedden, Dorothy and Heintzelman, Mark and Hunkapiller, Michael and Zoon, Kathryn (1984) Biologic activity in a fragment of recombinant human interferon α. Proceedings of the National Academy of Sciences of the United States of America, 81 (4). pp. 1045-1047. ISSN 0027-8424 http://resolver.caltech.edu/CaltechAUTHORS:ACKpnas84
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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.
| Item Type: | Article |
|---|---|
| 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. |
| Subject Keywords: | thermolysin; molecular sizes; partial amino acid sequence; antiviral activity |
| Record Number: | CaltechAUTHORS:ACKpnas84 |
| Persistent URL: | http://resolver.caltech.edu/CaltechAUTHORS:ACKpnas84 |
| Alternative URL: | http://www.pnas.org/cgi/content/abstract/81/4/1045 |
| Usage Policy: | No commercial reproduction, distribution, display or performance rights in this work are provided. |
| ID Code: | 8086 |
| Collection: | CaltechAUTHORS |
| Deposited By: | Tony Diaz |
| Deposited On: | 30 Jul 2007 |
| Last Modified: | 26 Dec 2012 09:36 |
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