1H nmr study of the effectiveness of various thiols for removal of methylmercury from hemolyzed erythrocytes

Dallas L. Rabenstein; R. Stephen Reid; Anvarhusein A. Isab

doi:10.1016/0162-0134(83)85006-5

¹H nmr study of the effectiveness of various thiols for removal of methylmercury from hemolyzed erythrocytes

Dallas L. Rabenstein^*, R. Stephen Reid, Anvarhusein A. Isab

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

26 Scopus citations

Abstract

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 α-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-dimercap-tosuccinic acid > mercaptosuccinic acid > cysteine > mercaptoacetic acid > D-penicillamine > 2, 3-dimercaptopropanesulfonic acid > N-acetyl-D,L-penicillamine > D.L-homocysteine.

Original language	English
Pages (from-to)	241-251
Number of pages	11
Journal	Journal of Inorganic Biochemistry
Volume	18
Issue number	3
DOIs	https://doi.org/10.1016/0162-0134(83)85006-5
State	Published - Jun 1983
Externally published	Yes

Bibliographical note

Funding Information:
This research was supported by the Natural Sciences and Engineering Research Council of Conada through their Strategic Grants Program and by the University of Alberta. Financial support by an I. W. h’iilam Scholarship (to R.S.R.) and by an Alberta He&age Foundation for Medical Research Postdoctoral Fellowship (to A.A.I.) is gratefully acknowledged.

ASJC Scopus subject areas

Biochemistry
Inorganic Chemistry

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10.1016/0162-0134(83)85006-5

Cite this

@article{8a90a9f971cf4cbe95a2ad963b724bea,

title = "1H nmr study of the effectiveness of various thiols for removal of methylmercury from hemolyzed erythrocytes",

abstract = "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 α-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-dimercap-tosuccinic acid > mercaptosuccinic acid > cysteine > mercaptoacetic acid > D-penicillamine > 2, 3-dimercaptopropanesulfonic acid > N-acetyl-D,L-penicillamine > D.L-homocysteine.",

author = "Rabenstein, \{Dallas L.\} and Reid, \{R. Stephen\} and Isab, \{Anvarhusein A.\}",

note = "Funding Information: This research was supported by the Natural Sciences and Engineering Research Council of Conada through their Strategic Grants Program and by the University of Alberta. Financial support by an I. W. h{\textquoteright}iilam Scholarship (to R.S.R.) and by an Alberta He\&age Foundation for Medical Research Postdoctoral Fellowship (to A.A.I.) is gratefully acknowledged.",

year = "1983",

month = jun,

doi = "10.1016/0162-0134(83)85006-5",

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journal = "Journal of Inorganic Biochemistry",

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AU - Rabenstein, Dallas L.

AU - Reid, R. Stephen

AU - Isab, Anvarhusein A.

N1 - Funding Information: This research was supported by the Natural Sciences and Engineering Research Council of Conada through their Strategic Grants Program and by the University of Alberta. Financial support by an I. W. h’iilam Scholarship (to R.S.R.) and by an Alberta He&age Foundation for Medical Research Postdoctoral Fellowship (to A.A.I.) is gratefully acknowledged.

PY - 1983/6

Y1 - 1983/6

N2 - 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 α-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-dimercap-tosuccinic acid > mercaptosuccinic acid > cysteine > mercaptoacetic acid > D-penicillamine > 2, 3-dimercaptopropanesulfonic acid > N-acetyl-D,L-penicillamine > D.L-homocysteine.

AB - 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 α-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-dimercap-tosuccinic acid > mercaptosuccinic acid > cysteine > mercaptoacetic acid > D-penicillamine > 2, 3-dimercaptopropanesulfonic acid > N-acetyl-D,L-penicillamine > D.L-homocysteine.

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