title: Isolation of the peptide inhibitor of H+-ATP synthase from Crithidia fasciculata and Trypanosoma cruzi.
abstract: 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.
authors.affiliation: Centro de Investigaciones Bioenergéticas, Facultad de Medicina, Buenos Aires, Argentina.
authors.forename: M C
authors.initials: MC
authors.lastname: Rilo
authors.forename: M A
authors.initials: MA
authors.lastname: Cataldi de Flombaum
authors.forename: A O
authors.initials: AO
authors.lastname: Stoppani
mesh_terms: 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
chemical_list: D011506:Proteins; D006180:Proton-Translocating ATPases; D014357:Trypsin; D000097795:ATPase Inhibitory Protein