Purification and Properties of Phosphofructokinase from Yeast

Abstract

Abstract A scheme has been devised for the purification of phosphofructokinase from bakers' yeast. The purified enzyme retains all the allosteric features observed for partially purified preparations of yeast phosphofructokinase. In contrast to mammalian phosphofructokinase, the yeast enzyme sediments as a single boundary with an s020,w of 17.8 S. The molecular weight was determined to be 5.84 ± 0.21 x 105 from sedimentation equilibrium measurements. The Michaelis constants of the substrates, the pH optima for catalysis, and the ultraviolet absorbance and electrophoretic properties of the purified enzyme are reported.