Purification and partial characterisation of and α-tocopherol-binding protein from rabbit heart cytosol

A K Dutta-Roy, M J Gordon, D J Leishman, B J Paterson, G G Duthie, W P T James

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An alpha-tocopherol-binding protein has been isolated and purified from rabbit heart cytosol. The purified protein had an apparent molecular mass of 14,200, as derived from SDS-PAGE. The content of the protein in rabbit heart was around 11.8 mug per g of tissue. The binding of alpha-tocopherol to the purified protein was rapid, reversible, and saturable. Neither gamma nor delta tocopherol could displace the bound alpha-tocopherol from the protein, suggesting a high specificity for alpha-tocopherol. Alpha-Tocopherol-binding protein did not bind oleate. Transfer of alpha-tocopherol from liposomes to mitochondria was stimulated 8-fold in the presence of the binding protein, suggesting that this protein may be involved in the intracellular transport of alpha-tocopherol in the heart.

Original languageEnglish
Pages (from-to)139-144
Number of pages6
JournalMolecular & Cellular Biochemistry
Issue number1-2
Publication statusPublished - 9 Jun 1993


  • D-alpha-tocopherol (vitamin-E)
  • alpha-tocopherol-binding protein
  • alpha-tocopherol transfer
  • rabbit heart
  • liposomes
  • FABP
  • rat-liver

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