Purification of the putative import-receptor for the precursor of the mitochondrial protein.

Abstract:

:The receptor protein for the mitochondrial protein precursor synthesized in the cytosol was extensively purified from the mitochondrial membrane fraction by affinity column chromatography using a synthetic peptide containing the extrapeptide of ornithine aminotransferase as a ligand. The purified fraction contained two major proteins with molecular masses of 52 and 29 kDa. Of these proteins, only the 29 kDa protein bound to the extrapeptide of ornithine aminotransferase. Furthermore, anti-29 kDa protein Fab fragments inhibited the import of pre-ornithine aminotransferase into mitochondria, suggesting that the 29 kDa protein plays an essential role in the process of import of the mitochondrial protein precursor.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Ono H,Tuboi S

doi

10.1093/oxfordjournals.jbchem.a123135

subject

Has Abstract

pub_date

1990-06-01 00:00:00

pages

840-5

issue

6

eissn

0021-924X

issn

1756-2651

journal_volume

107

pub_type

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