Abstract
Phosphofructokinase (ATP: d-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) was extracted from rat thymocytes and partially purified by the following steps: ammonium sulfate fractionation, heat treatment, TEAE-cellulose column chromatography and affinity chromatography on blue dextran polyacrylamide gel. Some properties of the enzyme thus obtained were compared with these of muscle phosphofructokinase. Thymocyte phosphofructokinase showed a higher affinity for TEAE cellulose, higher susceptibility to ATP inhibition, and greater sensitivity to allosteric effectors than the muscle enzyme. The concentration of fructose 6-phosphate required to give half-maximal velocity was higher for the thymocyte enzyme.
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