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

D. Blanchard, C. Bloy, P. Hermand, J. P. Cartron, A. M. Saboori, B. L. Smith, P. Agre

Research output: Contribution to journalArticlepeer-review

49 Scopus citations

Abstract

The 32,000 molecular weight (mol wt) erythrocyte Rh, D, c, and E polypeptides were seperately purified from cDE/cDE erythrocytes by monoclonal immunoprecipitations and compared by two-dimensional iodopeptide mapping. Digestions of the isolated Rh polypeptides with α-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 nonimmunologic protocol from cDE/cDE erythrocytes were virtually identical to the composite pattern (D + c + E) deduced from the individual maps of Rh D, c, and E iodopeptides. Digestions of the isolated Rh polypeptides with trypsin revealed an overall homology of approximately 50% between iodopeptides derived from D, c, and E. These data indicate that the erythrocyte Rh D, c, and E antigens are carried by homologous but distinct molecular species; c and E appear more closely related to each other than to D.

Original languageEnglish (US)
Pages (from-to)1424-1427
Number of pages4
JournalBlood
Volume72
Issue number4
DOIs
StatePublished - 1988
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Immunology
  • Hematology
  • Cell Biology

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