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

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 journal › Article › peer-review

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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title = "Properties of the retroviral proteinase from the Myeloblastosis Associated Virus",

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.",

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

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language = "English (US)",

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journal = "Journal of Bioactive and Compatible Polymers",

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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, M.

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.

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