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大鼠肝脏α-生育酚转运蛋白的纯化与鉴定

Purification and characterization of the alpha-tocopherol transfer protein from rat liver.

作者信息

Sato Y, Hagiwara K, Arai H, Inoue K

机构信息

Department of Health Chemistry, Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.

出版信息

FEBS Lett. 1991 Aug 19;288(1-2):41-5. doi: 10.1016/0014-5793(91)80999-j.

DOI:10.1016/0014-5793(91)80999-j
PMID:1879562
Abstract

alpha-Tocopherol transfer protein was purified from the 10,000 x 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.

摘要

α-生育酚转运蛋白是从大鼠肝脏10,000×g离心后的上清液中纯化得到的。该转运蛋白存在两种同工型,通过色谱聚焦法测定,其等电点分别为5.0和5.1。这两种同工型分子量相同;在SDS-聚丙烯酰胺凝胶电泳上均显示分子量约为30,500。通过氨基酸组成或底物特异性无法区分它们。

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