Abstract
DIPHTHERIA toxin causes the catalytic inactivation of polypeptide chain Elongation Factor 2 when the enzymically active N-terminal fragments of toxin, particularly fragment A, are mixed with broken cells of almost any eukaryotic source1–3 or when complete toxin molecules are incubated with intact susceptible cells4. Incubation of intact cells with fragment A does not lead to EF-2 inactivation. Probably, therefore, an apparatus exists in the membranes of susceptible cells that facilitates the uptake of toxin and generation of its fragment A in the cytoplasm and the entry process involves the C-terminal portion of the toxin molecule, fragment B (ref. 5).
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ITTELSON, T., GILL, D. Diphtheria Toxin: Specific Competition for Cell Receptors. Nature 242, 330–332 (1973). https://doi.org/10.1038/242330b0
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DOI: https://doi.org/10.1038/242330b0
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