Abstract
In vitro experiments with the isolated perfused rat heart and partially purified rat heart phosphofructokinase (PFK) have shown that the enzyme may be regulated by intracellular concentrations of adenine nucleotides, inorganic phosphate and citrate1–5. In particular, the acute changes which can be induced in PFK activity in the perfused heart by factors which inhibit respiratory chain phosphorylation and by the oxidation of fatty acids and ketone bodies have been attributed to changes in the concentration of these metabolites1–6. The activity of PFK is also diminished in perfused hearts taken from alloxan-diabetic and starved rats1–3. The effect of alloxan-diabetes has been attributed to inhibition of PFK by an increased concentration of citrate in the diabetic muscle2–6.
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