Purification of 52 kDa protein: a putative component of the import machinery for the mitochondrial protein-precursor in rat liver.
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.
Ono
H
H
Department of Biochemistry, Yamagata University School of Medicine, Japan.
Tuboi
S
S
D000818:Animals; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D007140:Immunoglobulin Fab Fragments / Q000378:metabolism; D008024:Ligands; D008099:Liver / Q000378:metabolism; D008565:Membrane Proteins / Q000302:isolation & purification* / Q000378:metabolism; D008930:Mitochondria, Liver / Q000737:chemistry*; D008970:Molecular Weight; D009953:Ornithine-Oxo-Acid Transaminase / Q000378:metabolism; D011498:Protein Precursors; D051381:Rats
D007140:Immunoglobulin Fab Fragments; D008024:Ligands; D008565:Membrane Proteins; D011498:Protein Precursors; D009953:Ornithine-Oxo-Acid Transaminase