Transferrin receptors on human B and T lymphoblastoid cell lines.
Experiments demonstrating the existence of receptors for iron-saturated transferrin on both B and T lymphoblastoid cell lines of human origin are described. Binding of 125I-labeled transferrin is rapid, saturable and reversible. It can be specifically inhibited by unlabeled transferrin but not by other proteins. The number of receptors on T cell lines determined by Scatchard analysis is almost double the number on B cell lines but the binding affinities are equal. The putative transferrin receptor can be removed from the cell by the proteolytic enzymes papain and trypsin, and is re-expressed during overnight incubation at 37 degrees C. Resynthesis is inhibited by puromycin. The receptor can be solubilized by deoxycholate, and retains transferrin binding capacity when non-covalently attached to an amphipathic matrix consisting of deoxycholate-coupled poly(L-lysyl) Agarose.
D001402:B-Lymphocytes / Q000378:metabolism*; D001665:Binding Sites; D002460:Cell Line; D006801:Humans; D010206:Papain; D011956:Receptors, Cell Surface / Q000302:isolation & purification / Q000378:metabolism*; D013601:T-Lymphocytes / Q000378:metabolism*; D014168:Transferrin / Q000378:metabolism*; D014357:Trypsin
D011956:Receptors, Cell Surface; D014168:Transferrin; D014357:Trypsin; D010206:Papain