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={T. Nishihara and H. Maeda and K. Okamoto and T. Oshida and T. Mizoguchi and T. 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… Expand
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References

SHOWING 1-10 OF 10 REFERENCES
Molecular and catalytic properties of purified glutathione S-transferase from human placenta.
TLDR
Glutathione S-transferase from human placenta has been purified with a simple and rapid method and the steady-state kinetics follow Michaelis-Menten kinetics and the conjugation reaction with 1-chloro-2,4-dinitrobenzene displays a random sequential mechanism. Expand
Glutathione S-transferases. The first enzymatic step in mercapturic acid formation.
TLDR
The purification of homogeneous glutathione S-transferases B and C from rat liver is described, and only transferases A and C are immunologically related. Expand
Nonequivalence of the two subunits of horse erythrocyte glutathione transferase in their reaction with sulfhydryl reagents.
TLDR
All the structural and kinetic data reported in this paper indicate a nonsymmetrical association of two identical subunits, or alternatively heterodimeric structure with subunits of very similar charge and size. Expand
Specific inactivation of glutathione S-transferases in class Pi by SH-modifiers.
TLDR
The present results suggest that the 47th cysteine residue may be located in the vicinity of the active site of Class Pi GSTs, and may be preferentially modified. Expand
The binding of substrates and a product of the enzymatic reaction to glutathione S-transferase A.
TLDR
The binding studies are fully consistent with a steady state random kinetic mechanism for the glutathione S-transferase A, and all ligands showed the same binding stoichiometry. Expand
Glutathione transferase from bovine placenta. Preparation, biochemical characterization, crystallization, and preliminary crystallographic analysis of a neutral class PI enzyme.
A method was developed to purify glutathione transferase from bovine placenta by affinity chromatography and fast protein liquid chromatography. The purified enzyme was homogeneous as judged byExpand
Glutathione transferases--structure and catalytic activity.
The glutathione transferases are recognized as important catalysts in the biotransformation of xenobiotics, including drugs as well as environmental pollutants. Multiple forms exist, and numerousExpand
The glutathione status of cells.
TLDR
GSH status, the biologically relevant chemistry of GSH, the forms in which GSH can be present within the cell, along with the GSH content of cells and the methods for analysis of this substance are discussed. Expand
Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation.
  • D. Ziegler
  • Chemistry, Medicine
  • Annual review of biochemistry
  • 1985
PERSPECTIVES AND SUMMARY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 306 REGULATION BY THIOL : DISULFIDE EXCHANGE-ANExpand
The isozymes of glutathion transferase
  • 1985