Abstract
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 language | English |
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Pages (from-to) | 139-144 |
Number of pages | 6 |
Journal | Molecular & Cellular Biochemistry |
Volume | 123 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - 9 Jun 1993 |
Keywords
- D-alpha-tocopherol (vitamin-E)
- alpha-tocopherol-binding protein
- alpha-tocopherol transfer
- rabbit heart
- liposomes
- FABP
- rat-liver