| Autor: |
Ackerman, S K, Zur Nedden, D, Heintzelman, M, Hunkapiller, M, Zoon, K |
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; February 1984, Vol. 81 Issue: 4 p1045-1047, 3p |
| Abstrakt: |
To attempt to locate functionally important regions of the interferon (IFN) molecule, recombinant human IFN-alpha 2 was subjected to proteolytic digestion. The bacterial proteinase thermolysin produced two major complementary fragments, HuIFN-alpha 2-(1-110) and HuIFN-alpha 2-(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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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