Related Experiment Video
Updated: Aug 16, 2026

Assembly and Purification of Prototype Foamy Virus Intasomes
Published on: March 19, 2018
Expression and characterization of human foamy virus proteinase
G Fenyöfalvi1, P Bagossi, T D Copeland
1Department of Biochemistry and Molecular Biology, University Medical School of Debrecen, Hungary.
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.
Related Concept Videos
Leaky Scanning
Mechanical Protein Function
Inhibitors Of Virion Release
Inhibitors of Virion Maturation and Assembly

