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

1988; Elsevier BV; Volume: 72; Issue: 4 Linguagem: Inglês

10.1182/blood.v72.4.1424.1424

1528-0020

Dominique Blanchard, C Bloy, Patricia Hermand, JP Cartron, AM Saboori, BL Smith, Peter Agre,

Advanced Proteomics Techniques and Applications

Abstract 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 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.