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dc.creatorBaker, Neil R.en_US
dc.creatorLietman, Paulen_US
dc.identifier.citationThe Ohio Journal of Science. v81, n2 (March, 1981), 74-77en_US
dc.descriptionAuthor Institution: Department of Microbiology, Ohio State University ; Division of Clinical Pharmacology, Johns Hopkins University School of Medicineen_US
dc.description.abstractThe extent of the transfer of the adenosine 5'-diphosphate ribose (ADPR) moiety of nicotinamide adenine dinucleotide onto elongation factor 2 (EF-2) catalyzed by Pseudomonas aeruginosa exotoxin A (PA-toxin) was dependent upon the presence of a reducing agent, dithiotheritol (DTT). The reaction requires DTT in low concentration (1 to 10 mM) and in the absence of DTT less product, ADPR-EF 2, was formed. PA-toxin was fully activated by treatment with a denaturing agent, sodium dodecyl sulphate (SDS), in conjunction with DTT. In the presence of activated toxin, the maximum transfer of ADPR onto EF-2 was observed when EF-2 had been previously reduced with DTT. Denaturation of EF-2 prior to reduction did not produce a further increase in its ability to act as a substrate for PA-toxin.en_US
dc.format.extent323335 bytes
dc.titleRequirement of Thiols in the Adenosine-Diphosphate Ribosylaton of Elongaton Factor-2 by Pseudomonas Aeruginosa Exotoxin Aen_US

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