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 |
|---|---|
| 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 |
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ASJC Scopus subject areas
- Biotechnology
- Biomaterials
- Materials Chemistry
- Polymers and Plastics
Cite this
Properties of the retroviral proteinase from the Myeloblastosis Associated Virus. / Strop, P.; Pichova, I.; Konvalinka, J.; Hruskova, O.; Blaha, I.; Andreansky, Martin; Fabry, M.; Horejsi, M.; Sedlacek, J.
In: Journal of Bioactive and Compatible Polymers, Vol. 6, No. 4, 01.10.1991, p. 339-347.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Properties of the retroviral proteinase from the Myeloblastosis Associated Virus
AU - Strop, P.
AU - Pichova, I.
AU - Konvalinka, J.
AU - Hruskova, O.
AU - Blaha, I.
AU - Andreansky, Martin
AU - Fabry, M.
AU - Horejsi, M.
AU - Sedlacek, J.
PY - 1991/10/1
Y1 - 1991/10/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0026239219&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026239219&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:0026239219
VL - 6
SP - 339
EP - 347
JO - Journal of Bioactive and Compatible Polymers
JF - Journal of Bioactive and Compatible Polymers
SN - 0883-9115
IS - 4
ER -