Abstract:
: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 submitochondrial particles and F1-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.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Igarashi K,Kashiwagi K,Kobayashi H,Ohnishi R,Kakegawa T,Nagasu A,Hirose Sdoi
10.1093/oxfordjournals.jbchem.a122847subject
Has Abstractpub_date
1989-08-01 00:00:00pages
294-8issue
2eissn
0021-924Xissn
1756-2651journal_volume
106pub_type
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