A high yield purification of the human transferrin receptor and properties of its major extracellular fragment

A. P. Turkewitz, J. F. Amatruda, D. Borhani, S. C. Harrison, A. L. Schwartz

Research output: Contribution to journalArticle

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Abstract

Human transferrin receptor is a disulfide-linked homodimer of 90-kDa glycoprotein subunits, capable of binding two transferrins. We report a new high yield affinity purification protocol for transferrin receptor from placenta which produces 3-4 mg of highly purified protein. Trypsin cleaves the protein at arginine-121, producing a stable fragment that contains 95% of the extracytoplasmic sequence; similar fragments are produced by several other proteases. The tryptic fragment is a nondisulfide-linked dimer in solution and binds two transferrin molecules. The dimensions of both the dimer fragment and its complex with transferrin are estimated by gel filtration.

Original languageEnglish (US)
Pages (from-to)8318-8325
Number of pages8
JournalJournal of Biological Chemistry
Volume263
Issue number17
StatePublished - Jan 1 1988

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Turkewitz, A. P., Amatruda, J. F., Borhani, D., Harrison, S. C., & Schwartz, A. L. (1988). A high yield purification of the human transferrin receptor and properties of its major extracellular fragment. Journal of Biological Chemistry, 263(17), 8318-8325.