Inactivation of human placenta glutathione S-transferase by SH/SS exchange reaction with biological disulfides.

@article{Nishihara1991InactivationOH,
  title={Inactivation of human placenta glutathione S-transferase by SH/SS exchange reaction with biological disulfides.},
  author={Tamao Nishihara and Hiroshi Maeda and Kazuki Okamoto and Tadahilo Oshida and Tadashi Mizoguchi and Tomoyuki Terada},
  journal={Biochemical and biophysical research communications},
  year={1991},
  volume={174 2},
  pages={580-5}
}
The oxidized glutathione inhibited the activity of glutathione S-transferase purified from human placenta just through competitive inhibition. On the other hand, cystine and cystamine inactivated the activity by pseudo first-order in low concentrations, accompanying the stoichiometric incorporation of the radioactivity of [14C]-cystine to the enzyme protein until a half mole per one subunit. This and the protective effect of glutathione analogues suggested that the SH/SS exchange reaction… CONTINUE READING

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