Literature DB >> 6248571

NAD turnover in microplasmodia of physarum polycephalum.

T Manser, B M Olivera, F B Haugli.   

Abstract

The rate of NAD turnover in microplasmodia of Physarum polycephalum was investigated using a double labeling technique with (14C)-adenine or adenosine and (3H)-nicotinamide. The half-life of an NAD molecule in Physarum was estimated to be 25 min, which is shorter than in either E. coli or human cell lines. The half-life of NAD in the presence of an inhibitor of NADase and poly ADPR synthase, 5-methylnicotinamide, was also investigated, but found to be indistinguishable from controls. The possible reasons for this and for the rapid turnover is discussed in the light of the known functions for NAD in prokaryotes and eukaryotes.

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Year:  1980        PMID: 6248571     DOI: 10.1002/jcp.1041020312

Source DB:  PubMed          Journal:  J Cell Physiol        ISSN: 0021-9541            Impact factor:   6.384


  3 in total

1.  A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family.

Authors:  J S Smith; C B Brachmann; I Celic; M A Kenna; S Muhammad; V J Starai; J L Avalos; J C Escalante-Semerena; C Grubmeyer; C Wolberger; J D Boeke
Journal:  Proc Natl Acad Sci U S A       Date:  2000-06-06       Impact factor: 11.205

2.  Telomeric and rDNA silencing in Saccharomyces cerevisiae are dependent on a nuclear NAD(+) salvage pathway.

Authors:  Joseph J Sandmeier; Ivana Celic; Jef D Boeke; Jeffrey S Smith
Journal:  Genetics       Date:  2002-03       Impact factor: 4.562

3.  Isolation of NAD cycle mutants defective in nicotinamide mononucleotide deamidase in Salmonella typhimurium.

Authors:  W Cheng; J Roth
Journal:  J Bacteriol       Date:  1995-12       Impact factor: 3.490

  3 in total

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