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.
Article|
November 01 1967
STUDIES ON THE MODE OF ACTION OF DIPHTHERIA TOXIN : IV. SPECIFICITY OF THE COFACTOR (NAD) REQUIREMENT FOR TOXIN ACTION IN CELL-FREE SYSTEMS
Ronald S. Goor,
Ronald S. Goor
From The Biological Laboratories, Harvard University, Cambridge, Massachusetts 02138
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A. M. Pappenheimer, Jr.
A. M. Pappenheimer, Jr.
From The Biological Laboratories, Harvard University, Cambridge, Massachusetts 02138
Search for other works by this author on:
Ronald S. Goor
From The Biological Laboratories, Harvard University, Cambridge, Massachusetts 02138
A. M. Pappenheimer, Jr.
From The Biological Laboratories, Harvard University, Cambridge, Massachusetts 02138
Received:
June 05 1967
Online ISSN: 1540-9538
Print ISSN: 0022-1007
Copyright © 1967 by The Rockefeller University Press
1967
J Exp Med (1967) 126 (5): 913–921.
Article history
Received:
June 05 1967
Citation
Ronald S. Goor, A. M. Pappenheimer; STUDIES ON THE MODE OF ACTION OF DIPHTHERIA TOXIN : IV. SPECIFICITY OF THE COFACTOR (NAD) REQUIREMENT FOR TOXIN ACTION IN CELL-FREE SYSTEMS . J Exp Med 1 November 1967; 126 (5): 913–921. doi: https://doi.org/10.1084/jem.126.5.913
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