1982
DOI: 10.1016/0167-4889(82)90038-6
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A proton nuclear magnetic resonance study of the binding of methylmercury in human erythrocytes

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Cited by 84 publications
(40 citation statements)
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“…There are no resonances which could be assigned to a dimethylarsinic(II1) moiety, which would be expected approximately 0.5 ppm upfield of the parent acid (11). The cysteinyl group (g2) of glutathione does not indicate any binding of arsenic through the sulfur (18). Therefore the reduction of dimethylarsinic acid by glutathione is unlikely to occur by direct reaction between the two compounds although it may occur indirectly via some membrane-mediated process (i.e., the arsenic acid remains extracellular).…”
Section: Resultsmentioning
confidence: 94%
See 1 more Smart Citation
“…There are no resonances which could be assigned to a dimethylarsinic(II1) moiety, which would be expected approximately 0.5 ppm upfield of the parent acid (11). The cysteinyl group (g2) of glutathione does not indicate any binding of arsenic through the sulfur (18). Therefore the reduction of dimethylarsinic acid by glutathione is unlikely to occur by direct reaction between the two compounds although it may occur indirectly via some membrane-mediated process (i.e., the arsenic acid remains extracellular).…”
Section: Resultsmentioning
confidence: 94%
“…Thus, the intensity and sign of this signal is a direct measure of the redox status of this molecule. Furthermore, direct binding of species like methylmercury to glutathione through the P-methylene group produces a specific change (nulling) in this residue (18), again indicating the sensitivity of this signal to molecular change.…”
Section: Resultsmentioning
confidence: 98%
“…Previous studies have estimated binding affinities of MMHg to small amino acids including glutamic acid and alanine in both laboratory settings (Corbeil et al, 1986;Alex and Savoie, 1987) and by using biological media such as human erythrocytes (Rabenstein et al, 1982). These studies have demonstrated that, while MMHg demonstrates appreciable binding affinity with these amino acids (Corbeil et al, 1986;Alex and Savoie, 1987), the binding affinity is weak enough to lessen MMHg transport to various biological tissues when compared to thiol-ligands (Rabenstein et al, 1982). Other amino acids examined by Bradley et al (2014) (i.e., glycine, lysine, serine, proline) displayed equally weak binding affinity with MMHg (Alex and Savoie, 1987).…”
Section: And Dmentioning
confidence: 99%
“…It can be metabolised (degraded) or it can interact with the cell macrostructure. Should the latter occur, the molecule will change relaxation time and would subsequently be expected to be filtered from the spectrum (Rabenstein et al, 1982). two effects on the HeLa cell.…”
mentioning
confidence: 99%