Abstract
A simplified method for the purification of human placental transferrin receptor is described. The procedure involves chromatography of a detergent extract of placenta on immobilized iron-loaded transferrin. Knowledge of the physiology of the interaction between transferrin and its receptor is applied to enable bound receptor to be eluted under mild conditions and essentially free of contaminating transferrin. Purified transferrin receptor and a monoclonal antibody to the receptor were used to developed a novel immunoradiometric assay for the receptor in which the monoclonal antibody is the radiolabelled species. A competition between two populations of receptor, one immobilized on a particulate support and the other in solution, provides the basis for the assay. Using this assay we have measured transferrin receptor levels in placental and hepatic tissue and in three cell lines during both the logarithmic and stationary phases of cell growth.
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