Redox forms of human placenta glutathione transferase.

@article{Ricci1991RedoxFO,
  title={Redox forms of human placenta glutathione transferase.},
  author={Giorgio Ricci and G del Boccio and Alfonso Pennelli and Mario Lo Bello and Raffaele Petruzzelli and Anna Maria Caccuri and Donatella Barra and Giorgio Federici},
  journal={The Journal of biological chemistry},
  year={1991},
  volume={266 32},
  pages={21409-15}
}
Human placenta glutathione transferase (EC 2.5.1.18) pi undergoes an oxidative inactivation which leads to the formation of an inactive enzymatic form which is homogeneous in several chromatographic and electrophoretic conditions. This process is pH dependent, and it occurs at appreciable rate in alkaline conditions and in the presence of metal ions. Dithiothreitol treatment completely restores the active form. -SH titration data and electrophoretic studies performed both on the oxidized and… CONTINUE READING

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By the use of a specific fluorescent thiol reagent the disulfide forming cysteines have been identified as the 47th and 101th residues .
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