Escherichia coli cells transformed with plasmids containing ricin B-chain coding sequences are shown to express this heterologous protein in inclusion bodies. After denaturation and renaturation of the product in the presence of glutathione and lactose, the recombinant ricin B-chain is soluble, biologically active and stable. Cytotoxicity of heterodimer with this protein and ricin A-chain is bound to be only ten times less than of native ricin. Recombinant B-chain alone was nontoxic to cells (ID50 > 10-6M). Our data suggest that N-glycosylation of ricin B-chain is not required for its biological activity.
|Original language||English (US)|
|Number of pages||8|
|Journal||Biochemistry and Molecular Biology International|
|State||Published - Jan 1 1994|
ASJC Scopus subject areas
- Molecular Biology