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Abstract
The state of intracellular Na+ in human and dog erythrocytes was characterized by 23Na-NMR using dysprosium complexes as shift reagents. Intracellular Na+ concentrations were determined using integration of the inner Na+ NMR signals and measurements of the intracellular volume using 59Co-NMR of extracellular Co(CN)3-6. T2 was found to be significantly shorter than T1, indicating some binding to macromolecules. While the longitudinal magnetization decay follows a single exponential, the transverse magnetization could be fitted with a double-exponential function. It was shown that neither the binding to the inner side of the membrane nor binding to hemoglobin contributes to the relaxation enhancement.
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