title: Interaction of F1-ATPase and its inhibitor peptide. Effect of pH.
abstract: 1. The inhibition of F1-ATPase by its natural peptide inhibitor is mixed non-competitive with two pH optimum values (5.5 and 8.2). 2. A two-step model for the interaction is suggested in which two enzyme conformations would exhibit different affinities for the peptide. 3. At low pH, interaction would be favoured. At high pH, a conformation (not susceptible to inhibition) changes into another (susceptible to inhibition) through the hydrolytic reaction stimulation, due to high pH.
authors.affiliation: Department of Biochemistry, University of Navarra, Pamplona, Spain.
authors.forename: C
authors.initials: C
authors.lastname: de Miguel
authors.forename: I
authors.initials: I
authors.lastname: Encío
authors.forename: N
authors.initials: N
authors.lastname: López-Mortalla
authors.forename: E
authors.initials: E
authors.lastname: Santiago
mesh_terms: D000818:Animals; D002417:Cattle; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008930:Mitochondria, Liver / Q000201:enzymology; D011506:Proteins / Q000378:metabolism*; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D051381:Rats; D000097795:ATPase Inhibitory Protein
chemical_list: D011506:Proteins; D006180:Proton-Translocating ATPases; D000097795:ATPase Inhibitory Protein