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- W13375610 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(-6)M). Our data suggest that N-glycosylation of ricin B-chain is not required for its biological activity." @default.
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- W13375610 date "1994-04-01" @default.
- W13375610 modified "2023-09-25" @default.
- W13375610 title "Renaturated ricin toxin B chain made in Escherichia coli is soluble, stable, and biologically active." @default.
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