Water transport across red-cell membranes following reductive methylation of the major transmembrane protein, band 3: Implications to increased divalent cation membrane permeability

Li Nan Chao, Mary Anne Yacko, Ping Zhuang, D. Allan Butterfield

Research output: Contribution to journalArticlepeer-review

Abstract

H-T-NMR methods in conjunction with normally membrane-impermeable Mn2+ were used to study the effect of reductive methylation of specific lysine residues of Band 3, the major transmembrane protein, on water permeability. At 21°C, the water apparent transverse relaxation time (T2) was decreased by nearly 16% (p < 00001) for cells with modified Band 3. Atomic absorption measurements of control and methylated cells showed an increased level of Mn2+ in the erythrocyte cytosol following methylation. This increased level of this paramagnetic relaxation agent is sufficient to relax interior water protein to the values obtained. Thus, following specific methylation of band 3, increased membrane permeability to divalent cations is observed. The results are discussed with reference to possible conformation changes of Band 3 following methylation, and the findings are interpreted be mean that the conformation of Band 3 has influence on cation permeability to erythrocyte membranes.

Original languageEnglish
Pages (from-to)107-116
Number of pages10
JournalMolecular Membrane Biology
Volume9
Issue number2
DOIs
StatePublished - 1990

Bibliographical note

Funding Information:
We thank Dr. Vahid Majidi for useful discussions on Mn2+ determinations. This work was supported in part by a grant from the National Science Foundation (RII-86-10671).

Keywords

  • Band 3
  • Erythrocyte membrane
  • Methylation
  • Paramagnetic relaxation
  • Water exchange rate

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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