Purification of phosphofructokinase from rabbit skeletal muscle based on its ability to aggregate in absence of its effectors.
Rabbit muscle phosphofructokinase was purified to homogeneity based on its property to form large aggregates with time at high concentration of its protein in absence of its effectors. The method involves no heat step or treatment with organic solvent or any ion-exchange columns. The enzyme thus prepared, however, exhibits the same kinetic properties as the enzyme purified by more drastic methods.
D000255:Adenosine Triphosphate; D000645:Ammonium Sulfate; D000818:Animals; D011232:Chemical Precipitation; D004591:Electrophoresis, Polyacrylamide Gel; D005615:Freezing; D006863:Hydrogen-Ion Concentration; D009132:Muscles / Q000201:enzymology*; D010732:Phosphofructokinase-1 / Q000302:isolation & purification*; D011817:Rabbits
D000255:Adenosine Triphosphate; D010732:Phosphofructokinase-1; D000645:Ammonium Sulfate