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Studies on the mode of action of diphtheria toxin. VII. Toxin-stimulated hydrolysis of nicotinamide adenine dinucleotide in mammalian cell extracts.
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MedLine Citation:
PMID:  4304436     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
When diphtheria toxin and NAD are added to soluble fractions containing aminoacyl transfer enzymes isolated from rabbit reticulocytes or from HeLa cells, free nicotinamide is released and, simultaneously, an inactive ADP ribose derivative of transferase II is formed. The reaction is reversible, and in the presence of excess nicotinamide, toxin catalyzes the restoration of aminoacyl transfer activity in intoxicated preparations. In living cultures of HeLa cells, the internal NAD concentration is sufficiently high to account for the rapid conversion, catalyzed by a few toxin molecules located in the cell membrane, of the entire cell content of free transferase II to its inactive ADP ribose derivative. Completely inactive ammonium sulfate fractions containing soluble proteins isolated from cells that have been exposed for several hours to excess toxin, can be reactivated to full aminoacyl transfer activity by addition of nicotinamide together with diphtheria toxin. Transferase II appears to be a highly specific substrate for the toxin-stimulated splitting of NAD and thus far no other protein acceptor for the ADP ribose moiety has been found.
Authors:
D M Gill; A M Pappenheimer; R Brown; J T Kurnick
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Journal of experimental medicine     Volume:  129     ISSN:  0022-1007     ISO Abbreviation:  J. Exp. Med.     Publication Date:  1969 Jan 
Date Detail:
Created Date:  1969-05-01     Completed Date:  1969-05-01     Revised Date:  2010-09-10    
Medline Journal Info:
Nlm Unique ID:  2985109R     Medline TA:  J Exp Med     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1-21     Citation Subset:  AIM; IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / metabolism
Animals
Carbon Isotopes
Chemical Phenomena
Chemistry
Culture Techniques
Diphtheria Toxin / pharmacology*
Electrophoresis
Hela Cells / drug effects*,  enzymology,  metabolism
Iodine Isotopes
NAD / metabolism*
Protein Biosynthesis*
Rabbits
Reticulocytes / enzymology
Transferases / metabolism
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Carbon Isotopes; 0/Diphtheria Toxin; 0/Iodine Isotopes; 53-84-9/NAD; EC 2.-/Transferases
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Full Text
Journal Information
Journal ID (nlm-ta): J Exp Med
ISSN: 0022-1007
ISSN: 1540-9538
Publisher: The Rockefeller University Press
Article Information
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Copyright © 1969 by The Rockefeller University Press
Received Day: 21 Month: 8 Year: 1968
Print publication date: Day: 1 Month: 1 Year: 1969
Volume: 129 Issue: 1
First Page: 1 Last Page: 21
ID: 2138597
PubMed Id: 4304436

STUDIES ON THE MODE OF ACTION OF DIPHTHERIA TOXIN : VII. TOXIN-STIMULATED HYDROLYSIS OF NICOTINAMIDE ADENINE DINUCLEOTIDE IN MAMMALIAN CELL EXTRACTS
D. Michael Gill
A. M. Pappenheimer, Jr.
Robin Brown
James T. Kurnick
From The Biological Laboratories, Harvard University, Cambridge, Massachusetts 02138


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