Kinetic studies of human polymorphonuclear leukocyte phosphofructokinase.

@article{Campos1991KineticSO,
  title={Kinetic studies of human polymorphonuclear leukocyte phosphofructokinase.},
  author={G. Rodrigues de Campos and Elena Ryder and Luz Marina Morales and Xiomara Raleigh},
  journal={Biochemical and biophysical research communications},
  year={1991},
  volume={178 2},
  pages={672-8}
}
Phosphofructokinase from human polymorphonuclear leukocytes has low cooperativity and high affinity for its substrate, F-6-P. It is resistant to ATP inhibition at pH 8; however, at pH 7.1 it becomes sensitive to the effect of this compound. It is activated by F-1, 6-P2; it is not very sensitive to citrate inhibition and F-2, 6-P2 has no effect on its activity. With these kinetic characteristics we assume that perhaps the predominant L-type subunit is accompanied by an F-type component. 

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