We studied the surfaces of maturing rabbit bone-marrow erythroid cells for the presence of the erythrocyte anion-transport protein by using an immunochemical method. An antibody was raised against the purified anion-transport protein. The antibody was shown to react specifically with the anion-transport protein and it recognized determinants in the extracellular as well as the cytoplasmic or intramembranous domains of the protein. The binding of the antibody to the surface of intact rabbit bone-marrow erythroid cells was studied by using the Staphylococcus aureus ‘rosette’ technique described by Gahmberg, Jokinen & Andersson [(1978) Blood 52, 379-386]. Although pronormoblasts had little of the protein, there was a progressive increase in the amount of the protein at the surface of cells of increasing maturity up to the reticulocyte stage. Most of the protein is inserted into the plasma membrane between the polychromatic-normoblast and reticulocyte stage of the cell.
Synthesis of the erythrocyte anion-transport protein. Immunochemical study of its incorporation into the plasma membrane of erythroid cells
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B M J Foxwell, M J A Tanner; Synthesis of the erythrocyte anion-transport protein. Immunochemical study of its incorporation into the plasma membrane of erythroid cells. Biochem J 1 April 1981; 195 (1): 129–137. doi: https://doi.org/10.1042/bj1950129
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