The cross-linking of 125I-labelled transferrin to rabbit reticulocytes.
125I-labelled transferrin has been covalently linked to proteins of rabbit reticulocyte membranes using three different cross-linking reagents: (a) bis(methyl) suberimidate (b) 4-methyl mercaptobutirimidate and (c) Cu-o-phenanthroline. Analysis of the products of the cross-linking reactions by SDS polyacrylamide gel electrophoresis revealed three radioactively labelled components. The major component corresponds to non-cross-linked transferrin while a second smaller component represents a complex (125 000 daltons) of membrane protein and transferrin. A third component (210 000 daltons) was observed when 4-methyl mercaptobutirimidate was used as a cross-linking reagent. The possibility that the two higher molecular weight complexes contain the receptor protein for transferrin is discussed.
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D004910:Erythrocyte Membrane / Q000378:metabolism; D007094:Imides; D008970:Molecular Weight; D010618:Phenanthrolines; D011817:Rabbits; D011955:Receptors, Drug / Q000378:metabolism*; D012156:Reticulocytes / Q000378:metabolism* / Q000648:ultrastructure; D014168:Transferrin / Q000378:metabolism*
D007094:Imides; D010618:Phenanthrolines; D011955:Receptors, Drug; D014168:Transferrin