Purification, and phosphorylation in vivo and in vitro, of phosphoenolpyruvate carboxykinase from cucumber cotyledons.

@article{Walker1995PurificationAP,
  title={Purification, and phosphorylation in vivo and in vitro, of phosphoenolpyruvate carboxykinase from cucumber cotyledons.},
  author={Robert Paul Walker and Richard C. Leegood},
  journal={FEBS letters},
  year={1995},
  volume={362 1},
  pages={
          70-4
        }
}
Phosphoenolpyruvate carboxykinase (PEPCK) with a subunit molecular mass of 74 kDa has been purified 450-fold to homogeneity from the cotyledons of cucumber (Cucumis sativus L.). This is the first purification of the native form of the enzyme from any plant tissue. Incubation of the purified enzyme with [gamma-32P]ATP and either phosphoenolpyruvate-carboxylase kinase or mammalian cAMP-dependent protein kinase led to labelling of the enzyme in a part of the molecule separate from the active site… CONTINUE READING
BETA

Citations

Publications citing this paper.
SHOWING 1-10 OF 17 CITATIONS

Light-regulated phosphorylation of maize phosphoenolpyruvate carboxykinase plays a vital role in its activity

  • Plant Molecular Biology
  • 2014
VIEW 4 EXCERPTS
CITES BACKGROUND & RESULTS
HIGHLY INFLUENCED

The Arabidopsis METACASPASE 9 Degradome

Liana Tsiatsiani, Evy Timmerman, +9 authors Frank Van Breusegema
  • 2013
VIEW 2 EXCERPTS
CITES BACKGROUND

Similar Papers

Loading similar papers…