A 1H nmr study of the interaction of aurothiomalate ("Myocrisin") with human red blood cells in vitro.

@article{Otiko1983A1N,
  title={A 1H nmr study of the interaction of aurothiomalate ("Myocrisin") with human red blood cells in vitro.},
  author={Gabriel Otiko and Muhammad Tahir Razi and Peter J. Sadler and A A Isab and Dallas L. Rabenstein},
  journal={Journal of inorganic biochemistry},
  year={1983},
  volume={19 3},
  pages={
          227-35
        }
}
The results of 1H spin-echo Fourier transform (SEFT) nuclear magnetic resonance (nmr) experiments suggest that some aurothiomalate binds intracellular glutathione (GSH) when added to suspensions of red cells in vitro. When added to red cell lysates, a specific binding of gold to cysteine of GSH is observed together with release of thiomalate. Gold binding to GSH can be reversed by addition of dimercaptopropanol sulfonate. Spectra are compared to those of an aurothiomalate-GSH model system. The… 
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  • Chemistry, Medicine
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  • 1992
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The interaction of gold(I) thiomalate (Autm) (Myocrysine) with ergothionine (ErSH) has been studied and it was found that ErSH forms a ternary complex of the type ErS-Au-tm at a 1:1 mole ratio; unlike other thiols it does not eject thiomicate (Htm) as a free ligand.
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There was a gradual decrease in the intensity of the GSH 1H spin-echo NMR resonances, but no new peaks were resolved, which was interpreted as formation of high-molecular weight Pt:GSH and mixed GS-Pt-S(hemoglobin) polymers.
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  • 1987
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THE REDOX REACTION OF GOLD(I)-THIOMALATE IN THE PRESENCE OF SELENOUREA
Abstract The interaction of thiourea (TU) and selenourea (SeU) with aurothiomalate (Autm) has been studied by 13C NMR spectroscopy. At a 1:1 ratio of TU:Autm, TU binds to Autm forming a ternary
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