H nmr study of the effectiveness of various thiols for removal of methylmercury from hemolyzed erythrocytes.
The effectiveness of eight thiol ligands for removing methylmercury (CH3Hg(II)) from its glutathione and hemoglobin complexes in hemolyzed erythrocytes has been studied by 1H nuclear magnetic resonance spectroscopy. These complexes are the predominant methylmercury species in human erythrocytes. The effectiveness was determined from the exchange-averaged chemical shift of the resonance for the proton on the alpha-carbon of the cysteinyl residue and from the intensity of the resonance for the methylene protons of the glycine residue of reduced glutathione (GSH), both of which provide a measure of the amount of glutathione in the CH3Hg(II)-complexed form. The thiol ligands were found to release GSH from its CH3Hg(II) complex in the order 2, 3-dimercaptosuccinic acid greater than mercaptosuccinic acid greater than cysteine greater than mercaptoacetic acid greater than D-penicillamine greater than 2,3-dimercaptopropanesulfonic acid greater than N-acetyl-D,L-penicillamine greater than D,L-homocysteine.
D004912:Erythrocytes / Q000187:drug effects*; D005978:Glutathione / Q000097:blood; D006454:Hemoglobins / Q000378:metabolism; D006461:Hemolysis; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008767:Methylmercury Compounds / Q000097:blood*; D013438:Sulfhydryl Compounds / Q000494:pharmacology*
D006454:Hemoglobins; D008767:Methylmercury Compounds; D013438:Sulfhydryl Compounds; D005978:Glutathione