Properties of the retroviral proteinase from the Myeloblastosis Associated Virus

P. Strop, I. Pichova, J. Konvalinka, O. Hruskova, I. Blaha, M. Andreansky, M. Fabry, M. Horejsi, J. Sedlacek

Research output: Contribution to journalArticle

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 languageEnglish (US)
Pages (from-to)339-347
Number of pages9
JournalJournal of Bioactive and Compatible Polymers
Volume6
Issue number4
StatePublished - Oct 1 1991
Externally publishedYes

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.