Thioltransferase in human red blood cells: kinetics and equilibrium.

@article{Mieyal1991ThioltransferaseIH,
  title={Thioltransferase in human red blood cells: kinetics and equilibrium.},
  author={J. Mieyal and D. Starke and S. A. Gravina and B. Hocevar},
  journal={Biochemistry},
  year={1991},
  volume={30 36},
  pages={
          8883-91
        }
}
  • J. Mieyal, D. Starke, +1 author B. Hocevar
  • Published 1991
  • Chemistry, Medicine
  • Biochemistry
  • 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… CONTINUE READING
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