Kinetics of Diphtheria Toxin Formation

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Diphtheria Disease and Genes Involved in Formation of Diphthamide, Key Effector of the Diphtheria Toxin

Shanow Uthman1, Shihui Liu2, Flaviano Giorgini1, Michael J. R. Stark3, Michael Costanzo4 and Raffael Schaffrath1,5 1Department of Genetics, University of Leicester, Leicester, 2Laboratory of Bacterial Diseases, NIAID, NIH, Bethesda, MD, 3Wellcome Trust Centre for Gene Regulation & Expression, University of Dundee, 4The Donnelly Centre, University of Toronto, Toronto, Ontario, 5Institut für Biol...

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Diphtheria Toxin In

Recent studies have demonstrated that diphtheria toxin is an enzyme of unusual type. Small amounts of the toxin, added to nicotinamide adenine dinucleotide (NAD)-containing mammalian cell extracts, block peptide-bond formation by catalyzing inactivation of the translocating enzyme, aminoacyltransferase 2 (T2) (1-3). This highly specific reaction involves the splitting of NAD with liberation of ...

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The Production of Diphtheria Toxin

Toxin of sufficient strength to kill a 400-gramme guinea-pig in three days and a half in a dose of 0.cubic centimetre developed in suitable bouillon, contained in ordinary Erlenmeyer flasks, within a period of twenty-four hours. In such boullon the toxin reached its greatest strength in from four to seven days (0.005 cubic centimetre killing a 500-gramme guinea-pig in three days). This period o...

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Ligand Interactions of Diphtheria Toxin

Prior studies have described two functionally distinct ligand-binding sites on whole diphtheria toxin, the NAD site, which catalyzes the intracellular ADP-ribosylation reaction, and the P site, which affects toxin binding to sensitive cells. Occupancy of the P site by ATP or other phosphorylated compounds inhibits toxin attachment to cells. Here we show that binding of NAD site and P site ligan...

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Identification of diphtheria toxin receptor and a nonproteinous diphtheria toxin-binding molecule in Vero cell membrane

Two substances possessing the ability to bind to diphtheria toxin (DT) were found to be present in a membrane fraction from DT-sensitive Vero cells. One of these substances was found on the basis of its ability to bind DT and inhibit its cytotoxic effect. This inhibitory substance competitively inhibited the binding of DT to Vero cells. However this inhibitor could not bind to CRM197, the produ...

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ژورنال

عنوان ژورنال: Journal of General Microbiology

سال: 1962

ISSN: 0022-1287

DOI: 10.1099/00221287-28-3-531