Thioltransferase in human red blood cells: kinetics and equilibrium.

@article{Mieyal1991ThioltransferaseIH,
  title={Thioltransferase in human red blood cells: kinetics and equilibrium.},
  author={John J. Mieyal and David W. Starke and Stephen Anthony Gravina and Barbara A Hocevar},
  journal={Biochemistry},
  year={1991},
  volume={30 36},
  pages={
          8883-91
        }
}
Thioltransferase from human red blood cells (HRBC TTase), coupled to GSSG reductase, catalyzed glutathione (GSH)-dependent reduction of prototype substrates hydroxyethyl disulfide (HEDS) and sodium S-sulfocysteine as well as of other homo- and heterodisulfides, including the protein mixed disulfide albumin-S-S-cysteine. Whereas apparent KM values for the substrates varied over more than a 20-fold range, the Vmax values agreed quite closely, usually within less than a factor of 2, suggesting… Expand
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