Separation, purification, and comparative properties of chloroplast and cytoplasmic phosphoglycerate kinase from barley leaves.

@article{McMorrow1990SeparationPA,
  title={Separation, purification, and comparative properties of chloroplast and cytoplasmic phosphoglycerate kinase from barley leaves.},
  author={E M McMorrow and J. William Bradbeer},
  journal={Plant physiology},
  year={1990},
  volume={93 2},
  pages={374-83}
}
The chloroplast and cytoplasmic isoenzymes of phosphoglycerate kinase (PGK) (EC. 2.7.2.3) from Hordeum vulgare leaves have been separated and purified for the first time to apparent homogeneity. The method for purifying the isoenzymes is described here and consists of DEAE Sephacel chromatography followed by affinity chromatography on ATP Sepharose. This consistently provided a 500- to 900-fold purification of each isoenzyme. Most of the total PGK in green barley leaves was found to be in the… CONTINUE READING