Abstract
Exposure of diphtheria toxin to dithiothreitol (and similar thiols) resulted in a subunit which was active in catalyzing the adenosine diphosphateribosylation of mammalian aminoacyl-transferase II in the presence of nicotinamide adenine dinucleotide. At the same time there was a marked increase in total ADP-ribosylation activity. A molecule which was apparently identical to the derived subunit in size and activity was detected in partially purified preparations of toxin.
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