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Expression and characterization of human foamy virus proteinase

  1. Author:
    Fenyofalvi, G.
    Bagossi, P.
    Copeland, T. D.
    Oroszlan, S.
    Boross, P.
    Tozser, J.

  2. Author Address

    Tozser J Debrecen Univ Med, Sch Med, Dept Biochem & Mol Biol POB 6 H-4012 Debrecen Hungary Debrecen Univ Med, Sch Med, Dept Biochem & Mol Biol H-4012 Debrecen Hungary NCI, Frederick Canc Res & Dev Ctr, ABL Basic Res Program, Special Program Prot Chem Frederick, MD 21702 USA NCI, Frederick Canc Res & Dev Ctr, ABL Basic Res Program, Mol Virol & Carcinogenesis Lab Frederick, MD 21702 USA
    1. Year: 1999
  2. Journal: Febs Letters
    1. 462
    2. 3
    3. Pages: 397-401
  4. Type of Article: Article
  1. Abstract:

    The human foamy virus proteinase was expressed in fusion with maltose binding protein in Escherichia coli and purified. The specific activity of the fusion protein was similar to that of the processed enzyme. The kinetic constants on foamy virus cleavage site substrates were very low but comparable to those obtained with the gag-encoded avian proteinase on its own substrates. The proteinase showed preference for high ionic strength and a pH optimum of 6.6. None of the tested retroviral cleavage site peptides were substrates, however, some peptides representing cleavage sites in retrotransposons were properly processed by the enzyme. (C) 1999 Federation of European Biochemical Societies. [References: 28]

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