Abstract
Transferrin receptor is isolated from the plasma membrane of chicken embryo red cell by affinity chromatography on transferrin-Sepharose 4B matrix. The molecular weight of the protein is approximately 58,000. The purified antibody to this protein is capable of agglutinating chicken embryo red cells, and the purified Fab fragments derived from this antibody are capable of inhibiting the antibody-induced agglutination, as well as the complement-induced hemolysis of chicken embryo red cells. The Fab fragments also inhibit the transferrin-mediated uptake of iron by chicken embryo red cells.
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Azari, P., Keung, WM. Isolation and characterization of transferrin receptor from embryonic chicken red cell. J Protein Chem 3, 19–33 (1984). https://doi.org/10.1007/BF01024834
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DOI: https://doi.org/10.1007/BF01024834