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

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 fusion proteins and measuring binding of fusion protein binding partners by GST pulldown assays, usually monitored by Western blot methodology.