| Autor: |
Dergousova, Natalya I., Amerik, Alexander Yu., Volynskaya, Alla M., Rumsh, Lev D. |
| Zdroj: |
Applied Biochemistry and Biotechnology; October 1996, Vol. 61 Issue: 1-2 p97-107, 11p |
| Abstrakt: |
A new method for obtaining HIV-I protease was suggested. Fusion proteins composed of the N-terminal fragment of human γ-interferon and HIV-I protease connected with (Asp)4Lys (protein I) or Asp-Pro (protein II) linkers were expressed inEscherichia colicells. The fusion proteins were produced as insoluble inclusion bodies in the 20% yield of total cell protein. Protein I was cleaved by enterokinase. The solubility of protein I was increased by treating with Nasulfite/Na-tetrathionate under denaturing conditions. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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