Glutathione-S-transferase-green fluorescent protein fusion protein reveals slow dissociation from high site density beads and measures free GSH.

@article{Tessema2006GlutathioneStransferasegreenFP,
  title={Glutathione-S-transferase-green fluorescent protein fusion protein reveals slow dissociation from high site density beads and measures free GSH.},
  author={Mathewos Tessema and Peter Carl Simons and Daniel F. Cimino and Lilliana Sanchez and Anna Waller and Richard G. Posner and Angela Wandinger-Ness and Eric R Prossnitz and Larry A. Sklar},
  journal={Cytometry. Part A : the journal of the International Society for Analytical Cytology},
  year={2006},
  volume={69 5},
  pages={
          326-34
        }
}
BACKGROUND Glutathione, a ubiquitous tripeptide, is an important cellular constituent, and measurement of reduced and oxidized glutathione is a measure of the redox state of cells. Glutathione-S-transferase (GST) fusion proteins bind naturally to beads derivatized with glutathione, and elution of such bead-bound fusion proteins with buffer containing millimolar glutathione is a commonly used method of protein purification. Many protein-protein interactions have been established by using GST… CONTINUE READING

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