Characterization and solubilization of the specific binding sites for d-alpha-tocopherol from human erythrocyte membranes.
Previous work from our laboratory has demonstrated the presence of specific binding sites for d-alpha-tocopherol (vitamin E) in intact human erythrocytes [A. E. Kitabchi and J. Wimalasena, Biochim. biophys. Acta 684, 300 (1982)]. The binding was time, temperature and cell concentration dependent. To localize the binding sites, red blood cells were further fractionated; greater than 90% of the tocopherol binding sites were localized on membranes. The washed membrane fraction from normal human erythrocytes has specific binding sites for d-alpha-tocopherol with properties suggestive of protein receptors. Two binding sites with Ka values of 3.31 x 10(1)M-1 and 1.51 x 10(6)M-1 were demonstrated, and solubilized d-alpha-tocopherol binding site complexes were resolved to a major component with an Mr of 65,000 and a minor component with an Mr of 125,000.
D001665:Binding Sites; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D017830:Octoxynol; D011092:Polyethylene Glycols; D012995:Solubility; D013696:Temperature; D014357:Trypsin; D014810:Vitamin E / Q000378:metabolism*
D014810:Vitamin E; D011092:Polyethylene Glycols; D017830:Octoxynol; D014357:Trypsin