Abstract
Abstract A simple procedure for purification of phosphofructokinase from rabbit erythrocytes was developed. The purified enzyme yields a single band on acrylamide gel electrophoresis. A schlieren pattern obtained from ultracentrifugation of the enzyme shows an asymmetrical peak and the major component has a sedimentation coefficient of 80 S. The results of sucrose density gradient centrifugation of fresh hemolysate show that the erythrocyte phosphofructokinase has a molecular weight of about 500,000. The molecular weight of dissociated enzyme in guanidine was determined to be approximately 53,000. Amino acid composition and a tryptic peptide map of erythrocyte phosphofructokinase are considerably different from those of skeletal muscle phosphofructokinase. Immunological reactivity of erythrocyte phosphofructokinase with antibody against muscle enzyme is less than that of muscle phosphofructokinase. Kinetic studies reveal that erythrocyte phosphofructokinase is inhibited by 2,3-diphosphoglycerate and that this inhibition is released by inorganic phosphate but not by AMP or ADP. Possible physiological significance of these observations is discussed.
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