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Science 6 June 1969:
Vol. 164. no. 3884, pp. 1179 - 1182
DOI: 10.1126/science.164.3884.1179
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Articles

Diphtheria Toxin Submit Active in vitro

R. J. Collier 1 and Heather A. Cole 1

1 Department of Bacteriology, University of California, Los Angeles

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.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Combining affinity purification by ADP-ribose-binding macro domains with mass spectrometry to define the mammalian ADP-ribosyl proteome.
N. Dani, A. Stilla, A. Marchegiani, A. Tamburro, S. Till, A. G. Ladurner, D. Corda, and M. Di Girolamo (2009)
PNAS 106, 4243-4248
   Abstract »    Full Text »    PDF »
Diphtheria: Recent studies have clarified the molecular mechanisms involved in its pathogenesis.
A. M. Pappenheimer Jr. and D. M. Gill (1973)
Science 182, 353-358
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Inactivation of Aminoacyl Transferase II by Diphtheria Toxin.
R. J. Collier and J. A. Traugh (1969)
Cold Spring Harb Symp Quant Biol 34, 589-594
   Abstract »    PDF »
Studies on Transferase II Using Diphtheria Toxin.
D. M. Gill, A. M. Pappenheimer Jr., and J. B. Baseman (1969)
Cold Spring Harb Symp Quant Biol 34, 595-602
   Abstract »    PDF »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)