Functional domains of the ATPase inhibitor protein from bovine heart mitochondria.
A study is presented of the activity and temperature dependence of the ATPase inhibitor protein (IF(1)) from bovine heart mitochondria and of synthetic partial IF(1) peptides. The results show that the IF(1)-(42-58) peptide is the most potent inhibitory domain of IF(1).
Zanotti
F
F
Department of Medical Biochemistry and Biology, University of Bari, Italy.
Raho
G
G
Vuolo
R
R
Gaballo
A
A
Papa
F
F
Papa
S
S
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors*; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D007425:Intracellular Membranes / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D008929:Mitochondria, Heart / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry* / Q000494:pharmacology; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D013816:Thermodynamics; D000097795:ATPase Inhibitory Protein
D000251:Adenosine Triphosphatases; D004791:Enzyme Inhibitors; D010446:Peptide Fragments; D011506:Proteins; D000097795:ATPase Inhibitory Protein