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Purification and characterization of the α‐tocopherol transfer protein from rat liver
Author(s) -
Sato Yuji,
Hagiwara Kenichi,
Arai Hiroyuki,
Inoue Keizo
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80999-j
Subject(s) - chromatofocusing , isoelectric point , isoelectric focusing , polyacrylamide gel electrophoresis , biochemistry , chemistry , gene isoform , molecular mass , chromatography , gel electrophoresis , microbiology and biotechnology , amino acid , enzyme , biology , gene
α‐Tocopheral transfer protein was purified from the 10 000 × g supernatant of rat liver. Two isoforms of the transfer protein exist, of which the isoelectric points are 5.0 and 5.1 as determined by chromatofocusing. These two isoforms have the same molecular weight; both showed molecular weight of approx. 30 500 on SDS‐polyacrylamide gel electrophoresis. They cannot be distinguished from each other by amino acid composition or substrate specificity.