Abstract
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) |
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Pages (from-to) | 1139-1146 |
Number of pages | 8 |
Journal | Biochemistry and Molecular Biology International |
Volume | 32 |
Issue number | 6 |
State | Published - 1994 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Genetics