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The Journal of Cell Biology, Vol 108, 2127-2135, Copyright © 1989 by The Rockefeller University Press

ARTICLES

Concentration of transferrin receptor in human placental coated vesicles

AP Turkewitz and SC Harrison
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts.

Coated vesicles were purified from human placenta by sedimentation, isopycnic centrifugation, and gel filtration. Quantitative Western blotting of the endogenous transferrin receptor (tfR) demonstrated the presence, on average, of roughly one receptor per vesicle. TfR appeared undersaturated with transferrin. After solubilizing vesicles in nonionic detergent, we looked for evidence of tfR interactions with other proteins. Solubilized tfR had an unexpectedly high mobility by gel filtration, apparently resulting from its self-association. This property was not seen in purified tfR or in tfR from a different cell fraction. The tfR complexes, though noncovalent, were largely resistant to conditions that disassemble coat proteins, and they did not appear to contain any other protein species.
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