Purification and properties of the F1-ATPase from liver mitochondria of Gallus gallus.
1. This paper is the first detailed report of the purification of a mitochondrial ATPase from an avian species. 2. The Gallus gallus liver mitochondrial F1-ATPase was purified by chloroform extraction and ion-exchange chromatography. 3. The enzyme shows the five alpha, beta, tau, delta, and epsilon subunits characteristic of mitochondrial F1-ATPases. 4. The Km for ATP is 1 mM and for Mg 0.5 mM with a specific activity of 25.2 mu moles of ATP hydrolyzed x min-1 x mg-1. 5. Unlike mammals enzymes the chicken mitochondrial ATPase shows maximal activity with ITP as substrate, and is strongly inhibited by Cu.
Lo Piero
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Istituto di Chimica agraria, Facoltà di Agraria, Università di Catania, Italy.
Petrone
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D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002413:Cations, Divalent; D002645:Chickens; D003300:Copper / Q000494:pharmacology; D007293:Inosine Triphosphate / Q000378:metabolism; D007700:Kinetics; D046911:Macromolecular Substances; D008930:Mitochondria, Liver / Q000201:enzymology*; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity
D002413:Cations, Divalent; D046911:Macromolecular Substances; D007293:Inosine Triphosphate; D003300:Copper; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases