Primary structure of alpha-tocopherol transfer protein from rat liver. Homology with cellular retinaldehyde-binding protein.
作者： Y. Sato , H. Arai , A. Miyata , S. Tokita , K. Yamamoto
DOI: 10.1016/S0021-9258(17)46761-5
关键词:
摘要: alpha-Tocopherol transfer protein (alpha TTP) present in rat liver cytosol specifically binds this vitamin and enhances its between separate membranes. We previously reported purification of alpha TTP showed that two isoforms exist liver, which the isoelectric points are 5.0 5.1, respectively (Sato, Y., Hagiwara, K., Arai, H., Inoue, K. (1991) FEBS Lett. 288, 41-45). In paper, we have isolated a cDNA clone with 2194 base pairs encoding from library. The amino acid sequence deduced contained all sequences peptide fragments obtained by digestion purified endoproteinase Lys-C. was found to encode isoform pI on basis cross-reactivity recombinant expressed Escherichia coli isoform-specific monoclonal antibody. From longest open reading frame cloned cDNA, one is predicted be composed 278 residues calculated molecular weight 31,845. Both Western Northern blot analyses revealed exclusively rats. has been exhibit structural homology cellular retinaldehyde-binding only visual tissues.
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