Effect of Polyamines on Mitochondrial F1-ATPase Catalyzed Reactions

The effect of polyamines on F1 -ATPase catalyzed reactions has been studied through the use of submitochondrial particles and F1 -ATPase. ATP degradation catalyzed by submitochon-drial particles and Fi-ATPase was inhibited by spermine and spermidine. Spermine's inhibition was much greater than...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1989-08, Vol.106 (2), p.294-298
Main Authors: Igarashi, Kazuei, Kashiwagi, Keiko, Kobayashi, Hiroshi, Ohnishi, Reiko, Kakegawa, Tomohito, Nagasu, Atsuko, Hirose, Seiyu
Format: Article
Language:English
Subjects:
Adenosine Diphosphate - metabolism
Adenosine Triphosphate - biosynthesis
Analytical, structural and metabolic biochemistry
Animals
Biogenic Polyamines - metabolism
Biogenic Polyamines - pharmacology
Biological and medical sciences
Cells, Cultured
Fundamental and applied biological sciences. Psychology
In Vitro Techniques
Kinetics
Mitochondria, Liver - drug effects
Mitochondria, Liver - enzymology
NADH, NADPH Oxidoreductases - metabolism
Non peptidic neurotransmitters, polyamines
Other biological molecules
Phospholipids - metabolism
Phosphorus Radioisotopes
Proton-Translocating ATPases - metabolism
Rats
Spermine - metabolism
Submitochondrial Particles - metabolism
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Summary:The effect of polyamines on F1 -ATPase catalyzed reactions has been studied through the use of submitochondrial particles and F1 -ATPase. ATP degradation catalyzed by submitochon-drial particles and Fi-ATPase was inhibited by spermine and spermidine. Spermine's inhibition was much greater than spermidine's effect. In contrast, P1-ATP exchange and succinate dependent ATP synthesis catalyzed by submitochondrial particles were both stimulated by spermine. The inhibition of ATPase activity by polyamines probably occurs through polyamine's replacement of Mg2+ on ATP, for the following reasons. (a) The ATPase activity inhibited by spermine was partially recovered when Mg2+ was added. (b) Spermine bound to ATP and phospholipids but not to F1 -ATPase; yet spermine inhibited the ATPase reaction catalyzed by F1-ATPase, a protein free of phospholipid. (c) The binding of spermine to ATP was inhibited by Mg2+. The ATP content in polyamine-deficient cells definitely was lower than that in normal cells. On the basis of these results, the possible role of spermine in keeping the ATP concentration at a high level is discussed.
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a122847