Identification of a low molecular mass (14.2 kDa) alpha-tocopherol-binding protein in the cytosol of rat liver and heart.
An alpha-tocopherol-binding protein (TBP) with a molecular mass of 14.2 kDa has been identified from the cytosol of rat heart and liver and purified to electrophoretic homogeneity by precipitation with 70% ammonium sulphate, followed by gel filtration and ion-exchange chromatography. In addition to the 14.2 kDa TBP, liver also contains the previously described 30 kDa TBP. The concentrations of the 14.2 kDa TBP in heart and liver were 12.3 micrograms and 17.5 micrograms per g of tissue, respectively. The purified protein specifically binds d alpha-tocopherol in preference to the delta- and gamma-homologues but does not bind oleate. The TBP stimulated the transfer of d alpha-tocopherol from liposomes to mitochondria in vitro by 8-10 fold. These results suggest that low molecular mass TBPs may play a role in intracellular vitamin E transport.
Dutta-Roy
A K
AK
Rowett Research Institute, Bucksburn, Aberdeen, Scotland, U.K.
Leishman
D J
DJ
Gordon
M J
MJ
Campbell
F M
FM
Duthie
G G
GG
D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003600:Cytosol / Q000378:metabolism; D008099:Liver / Q000378:metabolism*; D009206:Myocardium / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D013379:Substrate Specificity; D014462:Ultrafiltration; D014810:Vitamin E / Q000378:metabolism*
D002352:Carrier Proteins; C017763:alpha-tocopherol transfer protein; D014810:Vitamin E