Human erythrocyte band 3 polymorphism (band 3 Memphis): characterization of the structural modification (Lys 56----Glu) by protein chemistry methods.

@article{Yannoukakos1991HumanEB,
  title={Human erythrocyte band 3 polymorphism (band 3 Memphis): characterization of the structural modification (Lys 56----Glu) by protein chemistry methods.},
  author={D. Yannoukakos and C. Vasseur and C. Driancourt and Y. Blouquit and J. Delaunay and H. Wajcman and E. Bursaux},
  journal={Blood},
  year={1991},
  volume={78 4},
  pages={
          1117-20
        }
}
Band 3 variants occur rather frequently in different populations. Based on sodium dodecyl sulfate (SDS)-polyacrylamide electrophoretic properties, a widespread polymorphism (band 3 Memphis) has been previously described. It corresponds to a protein that has been hypothesized to be elongated in its N-terminal cytoplasmic domain. Band 3 from a heterozygote subject for this polymorphism and that displays a normal reactivity towards stilbene disulfonates has been isolated and its primary structure… Expand
69 Citations
High incidence of a polymorphic variant of erythrocyte membrane protein, Band 3-Memphis, on a western Japanese island
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