Two-dimensional iodopeptide mapping demonstrates that erythrocyte Rh D, c, and E polypeptides are structurally homologous but nonidentical.

@article{Blanchard1988TwodimensionalIM,
  title={Two-dimensional iodopeptide mapping demonstrates that erythrocyte Rh D, c, and E polypeptides are structurally homologous but nonidentical.},
  author={D. Blanchard and C. Bloy and P. Hermand and J. Cartron and A. M. Saboori and B. L. Smith and P. Agre},
  journal={Blood},
  year={1988},
  volume={72 4},
  pages={
          1424-7
        }
}
  • D. Blanchard, C. Bloy, +4 authors P. Agre
  • Published 1988
  • Medicine
  • Blood
  • The 32,000 molecular weight (mol wt) erythrocyte Rh D, c, and E polypeptides were separately purified from cDE/cDE erythrocytes by monoclonal immunoprecipitations and compared by two-dimensional iodopeptide mapping. Digestions of the isolated Rh polypeptides with alpha-chymotrypsin revealed a high degree of structural homology between c and E (13/14 iodopeptides were identical) and less striking homology between D and c or E (8/19 identical). The iodopeptide maps of Rh proteins purified by a… CONTINUE READING
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