Effect of polyamines on mitochondrial F-ATPase from Crithidia fasciculata and Trypanosoma cruzi.
ATP hydrolysis by Crithidia fasciculata mitochondrial ATPase was studied through the use of submitochondrial particles and the soluble enzyme. (a) ATP hydrolysis by these preparations was inhibited by spermine but not by spermidine or putrescine. (b) The ATPase activity inhibited by spermine was partially recovered when excess Mg2+ was added to the reaction mixture. (c) When polyamines were present throughout the preparation of the mitochondrial membranes, the membrane-bound ATPase was irreversibly inactivated. The polyamine effect decreased in the order spermine > putrescine > spermidine. (d) The spermidine or putrescine pre-treated membranes oxidized succinate at a faster rate than the control ones. (e) Trypanosoma cruzi F-ATPase was inhibited by polyamines in the same manner as the C. fasciculata enzyme.
Rilo
M C
MC
Centro de Investigaciones Bioenergéticas, Facultad de Medicina (UBA), Argentina.
Stoppani
A O
AO
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D016831:Crithidia fasciculata / Q000187:drug effects* / Q000201:enzymology; D006868:Hydrolysis; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008928:Mitochondria / Q000187:drug effects* / Q000201:enzymology; D011073:Polyamines / Q000494:pharmacology*; D011700:Putrescine / Q000494:pharmacology; D013095:Spermidine / Q000494:pharmacology; D013096:Spermine / Q000494:pharmacology; D014349:Trypanosoma cruzi / Q000187:drug effects* / Q000201:enzymology
D011073:Polyamines; D013096:Spermine; D000251:Adenosine Triphosphatases; D008274:Magnesium; D013095:Spermidine; D011700:Putrescine