Abstract
The proteinases from Myeloblastosis Associated Virus (MAV), Human Immunodeficiency Virus (HIV) and Bovine Leukemia Virus (BLV) were obtained by a massive heterologous expression in E. coli under T7 or tac promoter. All three proteinases were isolated to homogeneity, purified, and characterized. HIV-1 and MAV proteinases have very similar requirements for the subsites in S1 and S1' positions but have differences in the secondary sites S2 and S2'. The HIV-1 proteinase cleaves substrates with larger hydrophobic subsites in P2 and P2' (Leu, Ile) more readily than the MAV proteinase. The BLV proteinase, which prefers aliphatic side chains in P1 and P1', does not cleave MAV and HIV-1 consensus substrates.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 339-347 |
| Number of pages | 9 |
| Journal | Journal of Bioactive and Compatible Polymers |
| Volume | 6 |
| Issue number | 4 |
| State | Published - Oct 1 1991 |
| Externally published | Yes |
ASJC Scopus subject areas
- Bioengineering
- Biomaterials
- Polymers and Plastics
- Materials Chemistry
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Cite this
Strop, P., Pichova, I., Konvalinka, J., Hruskova, O., Blaha, I., Andreansky, M., Fabry, M., Horejsi, M., & Sedlacek, J. (1991). Properties of the retroviral proteinase from the Myeloblastosis Associated Virus. Journal of Bioactive and Compatible Polymers, 6(4), 339-347.