title: The isolation and partial characterization of transferrin binding components of the rabbit reticulocyte plasma membrane.
abstract: An affinity chromatograpy method utilising transferrin liganded agarose has been developed for the partial purification of transferrin binding components from Triton X-100 solubilised rabbit reticulocyte plasma membranes. A protein of molecular weight 30-35 000, shown to be located at the reticulocyte extra-cellular surface by lactoperoxidase 125I labelling, was isolated by the affinity method. The protein appeared to form a dimer of molecular weight 65-70 000 in Triton X-100 solution and was shown to associate with both 125I-labelled and unlabelled rabbit transferrin to form a high molecular weight complex in the same solution. N-[14C]Ethylmaleimide appeared to disrupt this association with transferrin and inhibit the formation of the dimer in Triton X-100 by binding to the protein. The protein appeared as a broad band of molecular weight 40 000 on sodium dodecyl sulphate polyacrylamide gel electrophoresis.
mesh_terms: D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification; D004910:Erythrocyte Membrane / Q000378:metabolism; D005033:Ethylmaleimide; D008565:Membrane Proteins / Q000097:blood* / Q000302:isolation & purification; D008970:Molecular Weight; D009975:Orthomyxoviridae / Q000201:enzymology*; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism*; D014168:Transferrin / Q000378:metabolism*
chemical_list: D002352:Carrier Proteins; D008565:Membrane Proteins; D014168:Transferrin; D005033:Ethylmaleimide