Isolation of tocopherol-binding proteins from the cytosol of smooth muscle A7r5 cells.
Cultured smooth muscle A7r5 cells were able to take up alpha-tocopherol (32 +/- 1.2 nmol/mg protein) the largest part of which (60%) was present in the cytosolic fraction. Using a tocopherol-based affinity chromatography and alpha-, beta-, gamma-, and delta-tocopherols as eluants, three polypeptides of molecular masses 81, 58 and 31 kDa were eluted. This preparation had alpha-[3H]tocopherol binding capability. The 58-kDa polypeptide could also be eluted by chromanol and the 81-kDa polypeptide could be eluted also by phytol. The 81-kDa polypeptide had the unique P-E-E-D-Q-X-Q-Y N-terminal sequence.
Nałecz
K A
KA
Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warsaw.
Nałecz
M J
MJ
Azzi
A
A
D000595:Amino Acid Sequence; D000818:Animals; D001013:Aorta, Thoracic / Q000737:chemistry / Q000196:embryology; D002352:Carrier Proteins / Q000737:chemistry / Q000302:isolation & purification*; D002460:Cell Line; D003600:Cytosol / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009131:Muscle, Smooth, Vascular / Q000737:chemistry*; D051381:Rats; D014810:Vitamin E / Q000378:metabolism
D002352:Carrier Proteins; C017763:alpha-tocopherol transfer protein; D014810:Vitamin E