The phosphofructokinase of Trypanosoma (Schizotrypanum) cruzi: purification and kinetic mechanism.

@article{Aguilar1986ThePO,
  title={The phosphofructokinase of Trypanosoma (Schizotrypanum) cruzi: purification and kinetic mechanism.},
  author={Z Aguilar and Julio Alberto Urbina},
  journal={Molecular and biochemical parasitology},
  year={1986},
  volume={21 2},
  pages={103-11}
}
The phosphofructokinase (ATP:D-fructose-6-phosphate 1-phosphotransferase, E.C.2.7.1.11) of Trypanosoma (Schizotrypanum) cruzi epimastigotes has been purified 180-fold, to apparent electrophoretic homogeneity, by differential centrifugation, gel filtration chromatography and anionic exchange chromatography. The minimum catalytic unit of the purified enzyme is a polypeptide of 17,000 +/- 1300 molecular weight, as shown by gel filtration chromatography and SDS-gel electrophoresis. Hanes-Woolf… CONTINUE READING