PMID: 4294108Nov 1, 1967Paper

Studies on the mode of action of diphtheria toxin. IV. Specificity of the cofactor (NAD) requirement for toxin action in cell-free systems

The Journal of Experimental Medicine
R S Goor, A M Pappenheimer

Abstract

The ability of a number of nucleotides related to NAD to replace NAD as cofactors for inhibition by diphtheria toxin of peptide bond formation has been examined. Neither NADH nor NADP are active. Of some 14 analogues closely related structurally to NAD that have been tested, only 3-thiocarboxamide pyridine-AD is as active as NAD itself. Replacement of the 3-carboxamide group on the pyridine ring by an acetyl group, or deamination of the purine ring, resulted in derivatives with reduced activity. The results were interpreted as suggesting that NAD and certain related nucleotides are capable of specific interaction with diphtheria toxin. Using the method of equilibrium dialysis, reversible binding of 1 mole of NAD per mole of toxin has been demonstrated. Toxoid does not interact with NAD.

References

Nov 1, 1967·The Journal of Experimental Medicine·R S Goor, A M Pappenheimer
Oct 8, 1962·Biochimica Et Biophysica Acta·J P HUMMEL, W J DREYER
Dec 1, 1964·The Journal of Experimental Medicine·R J COLLIER, A M PAPPENHEIMER

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Citations

Jan 1, 1978·Journal of Supramolecular Structure·M Vaughan, J Moss
Oct 1, 1998·Toxicology in Vitro : an International Journal Published in Association with BIBRA·E Chaves-OlarteM Thelestam
Feb 11, 2004·Clinical Oncology : a Journal of the Royal College of Radiologists·A J Chalmers
Jun 1, 1975·Proceedings of the National Academy of Sciences of the United States of America·D M Gill
Jan 1, 1976·Proceedings of the National Academy of Sciences of the United States of America·L Skogerson, E Wakatama
Jun 1, 1968·The Journal of Experimental Medicine·A M Pappenheimer, R Brown
Oct 10, 1968·Biochemical and Biophysical Research Communications·J A SchneiderE S Maxwell

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