Abstract
The binding of ^3H-d-α-tocopherol to isolated rat liver nuclei was investigated. 1) ^3H-d-α-Tocopherol rapidly bound to isolated nuclei and there seem to be specific binding sites for d-α-tocopherol in rat liver nuclei. 2) Nuclear membrane accounted for 90% of the total nuclear radioactivity found after the incubation of ^3H-d-α-tocopherol with rat liver nuclei. Subfractionation of nuclei revealed that nuclear matrix was the preferable binding sites of ^3H-d-α-tocopherol. 3) Dissociation of ^3H-d-α-tocopherol from nuclei by protease digestion suggested that α-tocopherol binds to proteins. 4) Subfractionation of chromatin further revealed that ^3H-d-α-tocopherol is associated with non-histone proteins having a high affinity for DNA.
