Abstract
Rat lung phosphofructokinase is purified 250-fold to a specific activity of about 10 by using ATP-sepharose affinity chromatography. The enzyme is activated by cyclic AMP, 5'-AMP, ADP, Pi, NH4+ and K+ ions. Depending upon the concentration of these effectors, the enzyme can exist in several interconvertible forms, differing widely in their affinity for fructose-6-P. These activators also overcome the inhibition of the enzyme by ATP and citrate, thus increasing the glycolytic rate in lung during hypoxia. Unlike the enzyme from other sources, the lung phosphofructokinase is not inhibited by cyclic GMP or phosphoenolpyruvate. The enzyme is very sensitive to inactivation by trypsin and this inactivation is completely reversed by assaying the proteolyzed enzyme in presence of its activators.
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