Several members of the RNase A superfamily are endowed with antitumor activ
ity, showing selective cytotoxicity toward several tumor cell lines. One of
these is onconase, the smallest member of the RNase A superfamily, which i
s at present undergoing phase III clinical trials. We report here the expre
ssion of recombinant onconase in Escherichia coli inclusion bodies, the cor
rect processing of the protein, followed by its purification in high yields
. The recombinant protein has biological and catalytic properties identical
to those of the natural enzyme. (C) 1999 Federation of European Biochemica
l Societies.