April 1976
Volume 15, Issue 4
Articles  |   April 1976
Properties of rat lens phosphofructokinase.
Investigative Ophthalmology & Visual Science April 1976, Vol.15, 279-287. doi:
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      H M Cheng, L T Chylack; Properties of rat lens phosphofructokinase.. Invest. Ophthalmol. Vis. Sci. 1976;15(4):279-287.

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      © ARVO (1962-2015); The Authors (2016-present)

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Two interconvertible forms of phosphofructokinase (PFK) have been eluted from a DEAE-cellulose column from the supernatant fraction of rat lens homogenates centrifuged at 96,000 x g for 1 hour at 0 to 4 degrees C. The interconversion can be manipulated by a change in the pH of the extracting and eluting buffers. PFK-I is the dominant form at pH between 7.4 to 7.05, while PFK-II dominates at pH 7.4 to 8.2. PFK-II is believed to be the functional form; it is inhibited by high concentrations of ATP and the inhibitory effect is enhanced by more acidic pH. Fructose-6-phosphate counteracts ATP inhibition, but the most potent de-inhibitors are ADP and AMP. Among the inorganic ions tested, sulfate, phosphate, ammonium, and potassium also de-inhibit, whereas calcium further inhibits the enzyme. The behavior of PFK under physiologic conditions and the significance of the presence of two forms of PFK in the lens are discussed.


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