A proton nuclear magnetic resonance study of the interaction of cadmium with human erythrocytes

Dallas L. Rabenstein; Anvarhusein A. Isab; Webe Kadima; P. Mohanakrishnan

doi:10.1016/0167-4889(83)90057-5

A proton nuclear magnetic resonance study of the interaction of cadmium with human erythrocytes

Dallas L. Rabenstein^*
, Anvarhusein A. Isab
, Webe Kadima
, P. Mohanakrishnan

^*Corresponding author for this work

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

49 Scopus citations

Abstract

The binding of Cd²⁺ by molecules in the intracellular region of human erythrocytes has been studied by ¹H-NMR spectroscopy. From changes in spin-echo Fourier transform NMR spectra for both intact and hemolyzed erythrocytes to which CdCl₂ was added, direct evidence was obtained for the binding of Cd²⁺ by intracellular glutathione and hemoglobin. Time-courses were measured by ¹H-NMR for the uptake of Cd²⁺ by intact erythrocytes in saline/glucose solution and in whole blood. In both cases, the uptake, as indicated by changes in the ¹H-NMR spectrum for intracellular glutathione, plateaus after about 30 min. The effectiveness of the disodium salt of EDTA and of various thiol-chelating agents for releasing glutathione from its Cd²⁺ complexes in hemolyzed erythrocytes was also studied. EDTA was found to be more effective than thiols, and dithiols more effective than monothiols.

Original language	English
Pages (from-to)	531-541
Number of pages	11
Journal	BBA - Molecular Cell Research
Volume	762
Issue number	4
DOIs	https://doi.org/10.1016/0167-4889(83)90057-5
State	Published - 14 Jul 1983
Externally published	Yes

Bibliographical note

Funding Information:
This research was supported by the University of Alberta and by a strategic grant from the Natural Sciences and Engineering Research Council of Canada (D.L.R.). A.A.I. was supported by an Alberta Heritage Foundation for Medical Research Postdoctoral Fellowship.

Keywords

(Human erythrocyte)
Cd
Glutathione
H-NMR
Ion-membrane interaction

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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10.1016/0167-4889(83)90057-5

Cite this

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title = "A proton nuclear magnetic resonance study of the interaction of cadmium with human erythrocytes",

abstract = "The binding of Cd2+ by molecules in the intracellular region of human erythrocytes has been studied by 1H-NMR spectroscopy. From changes in spin-echo Fourier transform NMR spectra for both intact and hemolyzed erythrocytes to which CdCl2 was added, direct evidence was obtained for the binding of Cd2+ by intracellular glutathione and hemoglobin. Time-courses were measured by 1H-NMR for the uptake of Cd2+ by intact erythrocytes in saline/glucose solution and in whole blood. In both cases, the uptake, as indicated by changes in the 1H-NMR spectrum for intracellular glutathione, plateaus after about 30 min. The effectiveness of the disodium salt of EDTA and of various thiol-chelating agents for releasing glutathione from its Cd2+ complexes in hemolyzed erythrocytes was also studied. EDTA was found to be more effective than thiols, and dithiols more effective than monothiols.",

keywords = "(Human erythrocyte), Cd, Glutathione, H-NMR, Ion-membrane interaction",

author = "Rabenstein, \{Dallas L.\} and Isab, \{Anvarhusein A.\} and Webe Kadima and P. Mohanakrishnan",

note = "Funding Information: This research was supported by the University of Alberta and by a strategic grant from the Natural Sciences and Engineering Research Council of Canada (D.L.R.). A.A.I. was supported by an Alberta Heritage Foundation for Medical Research Postdoctoral Fellowship.",

year = "1983",

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AU - Rabenstein, Dallas L.

AU - Isab, Anvarhusein A.

AU - Kadima, Webe

AU - Mohanakrishnan, P.

N1 - Funding Information: This research was supported by the University of Alberta and by a strategic grant from the Natural Sciences and Engineering Research Council of Canada (D.L.R.). A.A.I. was supported by an Alberta Heritage Foundation for Medical Research Postdoctoral Fellowship.

PY - 1983/7/14

Y1 - 1983/7/14

N2 - The binding of Cd2+ by molecules in the intracellular region of human erythrocytes has been studied by 1H-NMR spectroscopy. From changes in spin-echo Fourier transform NMR spectra for both intact and hemolyzed erythrocytes to which CdCl2 was added, direct evidence was obtained for the binding of Cd2+ by intracellular glutathione and hemoglobin. Time-courses were measured by 1H-NMR for the uptake of Cd2+ by intact erythrocytes in saline/glucose solution and in whole blood. In both cases, the uptake, as indicated by changes in the 1H-NMR spectrum for intracellular glutathione, plateaus after about 30 min. The effectiveness of the disodium salt of EDTA and of various thiol-chelating agents for releasing glutathione from its Cd2+ complexes in hemolyzed erythrocytes was also studied. EDTA was found to be more effective than thiols, and dithiols more effective than monothiols.

AB - The binding of Cd2+ by molecules in the intracellular region of human erythrocytes has been studied by 1H-NMR spectroscopy. From changes in spin-echo Fourier transform NMR spectra for both intact and hemolyzed erythrocytes to which CdCl2 was added, direct evidence was obtained for the binding of Cd2+ by intracellular glutathione and hemoglobin. Time-courses were measured by 1H-NMR for the uptake of Cd2+ by intact erythrocytes in saline/glucose solution and in whole blood. In both cases, the uptake, as indicated by changes in the 1H-NMR spectrum for intracellular glutathione, plateaus after about 30 min. The effectiveness of the disodium salt of EDTA and of various thiol-chelating agents for releasing glutathione from its Cd2+ complexes in hemolyzed erythrocytes was also studied. EDTA was found to be more effective than thiols, and dithiols more effective than monothiols.

KW - (Human erythrocyte)

KW - Cd

KW - Glutathione

KW - H-NMR

KW - Ion-membrane interaction

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DO - 10.1016/0167-4889(83)90057-5

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JO - BBA - Molecular Cell Research

JF - BBA - Molecular Cell Research

IS - 4

ER -

A proton nuclear magnetic resonance study of the interaction of cadmium with human erythrocytes

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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