Steady-state kinetics of F1-ATPase: mechanism of anion activation

The kinetic behaviour of the ATPase activity of beef heart F1 depends largely on the exposure of the enzyme to some anionic ligands such as sulphate and/or EDTA. F1 prepared in the presence of such anions exhibited a triphasic kinetic pattern whereas F1 from which those anions were removed by dialys...

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Veröffentlicht in:	FEBS letters 1985-11, Vol.192 (1), p.123-127
Hauptverfasser:	ROVERI, O. A, CALCATERRA, N. B
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Diphosphate - metabolism Adenosine Triphosphate - metabolism Analytical, structural and metabolic biochemistry Animals Anions - pharmacology Bicarbonates - pharmacology Biological and medical sciences Cattle Dialysis Edetic Acid - pharmacology Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrolases Kinetics Myocardium - enzymology Proton-Translocating ATPases - metabolism Sulfates - pharmacology
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