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Purification of 52 kDa protein: a putative component of the import machinery for the mitochondrial protein-precursor in rat liver.

作者信息

Ono H, Tuboi S

机构信息

Department of Biochemistry, Yamagata University School of Medicine, Japan.

出版信息

Biochem Biophys Res Commun. 1991 Oct 15;180(1):450-4. doi: 10.1016/s0006-291x(05)81314-2.

DOI:10.1016/s0006-291x(05)81314-2
PMID:1930237
Abstract

A protein having a molecular mass of 52 kDa was purified to homogeneity from solubilized mitochondrial membrane proteins by affinity column chromatography using the synthetic presequence of ornithine aminotransferase (OAT) as the ligand. This 52 kDa protein was specifically bound to the affinity column and eluted with 1 mM OAT-presequence, indicating that it recognized the presequence and bound to it specifically. Anti-52 kDa protein Fab fragments specifically inhibited the import of OAT-precursor into mitochondria, showing that the 52 kDa protein plays an essential role in this process. These results suggest that 52 kDa protein is a component of the import machinery of the mitochondrial protein-precursor in the mitochondrial membrane.

摘要

相似文献

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引用本文的文献

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Mitochondrial protein import: specific recognition and membrane translocation of preproteins.线粒体蛋白质输入:前体蛋白的特异性识别与膜易位
J Membr Biol. 1993 Sep;135(3):191-207. doi: 10.1007/BF00211091.