Reticulocyte membrane transferrin receptors.
A membrane protein with specific transferrin binding activity has been isolated from rabbit reticulocytes. The isolation procedure involved the immunoprecipitation by antibody to transferrin of transferrin-receptor complexes from reticulocyte membrane proteins which had been solubilized with nonionic detergent. Receptor dissociated from the antibody-transferrin-receptor complexes could bind transferrin saturably and reversibly. It migrated electrophoretically as a single band of glycoprotein with an estimated molecular weight of approximately 180 000 which was reduced to around 93 000 following complete dissociation with dithiothreitol.
D000818:Animals; D011232:Chemical Precipitation; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008565:Membrane Proteins / Q000097:blood / Q000302:isolation & purification*; D011092:Polyethylene Glycols; D011817:Rabbits; D011863:Radioimmunoassay; D011956:Receptors, Cell Surface / Q000302:isolation & purification* / Q000378:metabolism; D012156:Reticulocytes / Q000032:analysis* / Q000378:metabolism; D012995:Solubility; D014168:Transferrin / Q000378:metabolism*
D008565:Membrane Proteins; D011956:Receptors, Cell Surface; D014168:Transferrin; D011092:Polyethylene Glycols