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Expression and characterization of human foamy virus proteinase
Author(s) -
Fenyöfalvi György,
Bagossi Péter,
Copeland Terry D.,
Oroszlan Stephen,
Boross Péter,
Tözsér József
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01563-x
Subject(s) - maltose binding protein , cleavage (geology) , enzyme , fusion protein , biochemistry , chemistry , virus , ionic strength , escherichia coli , microbiology and biotechnology , tobacco etch virus , proteinase k , biology , recombinant dna , virology , plant virus , gene , potyvirus , paleontology , fracture (geology) , aqueous solution
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.