NAD turnover in microplasmodia ofphysarum polycephalum
- 1 March 1980
- journal article
- research article
- Published by Wiley in Journal of Cellular Physiology
- Vol. 102 (3) , 379-384
- https://doi.org/10.1002/jcp.1041020312
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‐methyl‐nicotinamide, 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.This publication has 15 references indexed in Scilit:
- Turnover of nicotinamide adenine dinucleotide in cultures of human cellsJournal of Cellular Physiology, 1976
- Pyridine nucleotide metabolism in imaginal discs of Drosophila melanogasterBiochemical Genetics, 1976
- Magnitude and significance of NAD turnover in human cell line D98/AH2Nature, 1976
- Poly(ADP-ribose) and ADP-ribosylation of proteinsPublished by Springer Nature ,1976
- Poly(adenosine diphosphate ribose) polymerase in Physarum polycephalumBiochemical Journal, 1975
- The biosynthesis and turnover of nicotinamide adenine dinucleotide in enucleated culture cellsJournal of Cellular Physiology, 1974
- Pyridine nucleotide metabolism in mammalian cells in cultureJournal of Cellular Physiology, 1973
- Inhibition of nuclear NAD nucleosidase and poly ADP-ribose polymerase activity from rat liver by nicotinamide and 5′-methyl nicotinamideBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1971
- A gene conferring actidione resistance and abnormal morphology onPhysarum polycephalumplasmodiaGenetics Research, 1970
- Nicotinamide from Nicotinonitrile by Catalytic HydrationJournal of the American Chemical Society, 1948