A 23Na multiple-quantum-filtered NMR study of the effect of the cytoskeleton conformation on the anisotropie motion of sodium ions in red blood cells

Tatyana Knubovets*, Hadassah Shinar, Uzi Eliav, Gil Navon

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Recently, it has been shown that 23Na double-quantum-filtered NMR spectroscopy can be used to detect anisotropic motion of bound sodium ions in biological systems. The technique is based on the formation of the second-rank tensor when the quadrupolar interaction is not averaged to zero. Using this method, anisotropic motion of bound sodium in human and dog red blood cells was detected, and the effect was shown to depend on the integrity of the membrane cytoskeleton. In the present study, multiplequantum-flltered techniques were applied in combination with a quadrupolar echo to measure the transverse-relaxation times, T2t and J2s- Line fitting was performed to obtain the values of the residual quadrupolar interaction, which was measured for sodium in a variety of mammalian erythrocytes of different size, shape, rheological properties, and sodium concentrations. Human unsealed white ghosts were used to study sodium bound at the anisotropic sites on the inner side of the RBC membrane. Modulations of the conformation of the cytoskeleton by the variation of either the ionic strength or pH of the suspending medium caused drastic changes in both the residual quadrupolar interaction and T2r due to changes in the fraction of bound sodium ions as well as changes in the structure of the binding sites. By combining the two spectroscopic parameters, structural change can be followed. The changes in the structure of the sodium anisotropic binding sites deduced by this method were found to correlate with known conformational changes of the membrane cytoskeleton. Variations of the medium pH affected both the fraction of bound sodium ions and the structure of the anisotropic binding sites. Sodium and potassium were shown to bind to the anisotropic binding sites with the same affinity, e 1996 Academic Press, Inc.

Original languageEnglish
Pages (from-to)16-25
Number of pages10
JournalJournal of Magnetic Resonance - Series B
Volume110
Issue number1
DOIs
StatePublished - 1996

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