A proton nuclear magnetic resonance study of the binding of methylmercury in human erythrocytes
- 1 February 1982
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Vol. 720 (1) , 53-64
- https://doi.org/10.1016/0167-4889(82)90038-6
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- Nuclear magnetic resonance studies of the solution chemistry of metal complexes. XVII. Formation constants for the complexation of methylmercury by sulfhydryl-containing amino acids and related moleculesCanadian Journal of Chemistry, 1981
- Nuclear magnetic resonance studies of the complexation of trimethyllead by glutathione in aqueous solution and in intact human erythrocytesJournal of the American Chemical Society, 1981
- The incorporation of 2h‐labelled glycine into the glutathione of intact human erythrocytes studied by 1h spin‐echo fourier transform NMRFEBS Letters, 1979
- The mobility of methylmercury in biological systemsBioinorganic Chemistry, 1978
- The aqueous solution chemistry of methylmercury and its complexesAccounts of Chemical Research, 1978
- Human erythrocyte metabolism studies by 1H spin echo NMRFEBS Letters, 1977
- Pulse methods for the simplification of protein NMR spectraFEBS Letters, 1975
- Nuclear magnetic resonance studies of the solution chemistry of metal complexes. XI. Binding of methylmercury by sulfhydryl-containing amino acids and by glutathioneJournal of the American Chemical Society, 1975
- Effect of glutathione depletion on tissue deposition of methylmercury in ratsToxicology and Applied Pharmacology, 1975
- Association Constants of Methylmercury with Sulfhydryl and Other BasesJournal of the American Chemical Society, 1961