Determination of the orientation of a band 3 affinity spin-label relative to the membrane normal axis of the human erythrocyte.

@article{Hustedt1996DeterminationOT,
  title={Determination of the orientation of a band 3 affinity spin-label relative to the membrane normal axis of the human erythrocyte.},
  author={Eric J. Hustedt and Albert H. Beth},
  journal={Biochemistry},
  year={1996},
  volume={35 21},
  pages={
          6944-54
        }
}
The orientation of the nitroxide moiety of an isotopically substituted spin-labeled derivative of dihydrostilbenedisulfonate ([15N,2H13]-SL-H2DADS-maleimide) covalently coupled at the extracellular stilbenedisulfonate binding site of the human erythrocyte anion exchange protein, band 3, has been determined relative to the membrane normal axis of intact cells. The X-band linear electron paramagnetic resonance (EPR) spectra of [15N,2H13]-SL-H2DADS-maleimide-labeled band 3 in intact erythrocytes… CONTINUE READING
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