Comparison of properties of mistletoe lectin I A-chain and ricin B-chain conjugate with native toxins

Journal/Book: FEBS Letters 336 (1), 100-102. 1993;

Abstract: Chimeric toxin protein was prepared from the mistletoe lectin I A-chainand ricin B-chain by using the disulfide exchange reaction. Ricin andchimeric protein were indistinguishable in binding to immobilizedasialofetuin in ELISA. Chimeric protein was more toxic to Jurkat cellsthan native mistletoe lectin I, but not so effective as native ricin. Inthe presence of NH4Cl, which enhances the toxicity of some toxins andimmunotoxins, but does not influence ricin toxicity, both ricin andchimeric toxin had equal cytotoxic activity. The possibility isdiscussed that the ricin B-chain protects the ricin A-chain (RTA) fromdegradation during delivering RTA from the cell surface to the placewhere RTA is translocated into the cytosol. Author.

Keyword(s): CELL-LINE

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