Isolation of the peptide inhibitor of H+-ATP synthase from Crithidia fasciculata and Trypanosoma cruzi.
An inhibitor of Crithidia fasciculata and Trypanosoma cruzi H+ -ATP synthase (ATPase) was isolated from these organims mitochondrial particles, either by (a) ammonium sulfate-cholate extraction followed by heat treatment and ethanol precipitation, or (b) gel-filtration on Sephadex G-50, followed by a similar purification procedure. Inactivation by trypsin supported the inhibitor peptide structure. Removal of the peptide inhibitor increased about three-fold the specific activity of the protozoan ATPases. The isolated peptides and a highly purified bovine heart ATPase inhibitor inhibited C. fasciculata ATPase as a function of the peptide concentration.
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Centro de Investigaciones Bioenergéticas, Facultad de Medicina, Buenos Aires, Argentina.
Cataldi de Flombaum
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Stoppani
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D000818:Animals; D002417:Cattle; D005591:Chemical Fractionation; D002850:Chromatography, Gel; D003421:Crithidia / Q000032:analysis* / Q000201:enzymology; D008928:Mitochondria / Q000032:analysis; D011506:Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors*; D014349:Trypanosoma cruzi / Q000032:analysis* / Q000201:enzymology; D014357:Trypsin; D000097795:ATPase Inhibitory Protein
D011506:Proteins; D006180:Proton-Translocating ATPases; D014357:Trypsin; D000097795:ATPase Inhibitory Protein