Effective expression and purification of recombinant onconase, an antitumor protein

Citation
E. Notomista et al., Effective expression and purification of recombinant onconase, an antitumor protein, FEBS LETTER, 463(3), 1999, pp. 211-215
Citations number
21
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
00145793 → ACNP
Volume
463
Issue
3
Year of publication
1999
Pages
211 - 215
Database
ISI
SICI code
0014-5793(199912)463:3<211:EEAPOR>2.0.ZU;2-G
Abstract
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.