| Autor: |
Blanchard, Dominique, Bloy, Christian, Hermand, Patricia, Cartron, Jean-Pierre, Saboori, Ali M., Smith, Barbara L., Agre, Peter |
| Zdroj: |
Blood; October 1988, Vol. 72 Issue: 4 p1424-1427, 4p |
| Abstrakt: |
The 32,000 molecular weight (mol wt) erythrocyte Rh D, c, end E polypeptides were separately purified from cDE/cDE erythrocytes by monoclonel immunoprecipitetions end compered by two-dimensional iodopeptide mapping. Digestions of the isoleted Rh polypeptides with a-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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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