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Mol. Cell. Biochem. · Jun 1993
Purification and partial characterisation of an alpha-tocopherol-binding protein from rabbit heart cytosol.
- A K Dutta-Roy, M J Gordon, D J Leishman, B J Paterson, G G Duthie, and W P James.
- Division of Biochemical Sciences, Rowett Research Institute, Aberdeen, Scotland, UK.
- Mol. Cell. Biochem. 1993 Jun 9; 123 (1-2): 139-44.
AbstractAn 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 micrograms 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.
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