Partial purification of the receptor protein essential for import of pre-ornithine aminotransferase into mitochondria.
The isolated mitochondrial outer membrane fraction strongly inhibits the import of pre-ornithine aminotransferase, but other membranes such as rough microsomes did not. This inhibition seems to be caused by a receptor in the isolated outer membrane which binds competitively pre-ornithine aminotransferase. The mitochondrial outer membrane could be solubilized using detergent. And a receptor for pre-ornithine aminotransferase was partially purified by ammonium sulfate fractionation followed by column chromatography on Sephacryl S-300. Liposomes reconstituted from the partially purified receptor and lecithin could inhibit the import of pre-ornithine aminotransferase into mitochondria and bind the precursor.
D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification / Q000378:metabolism*; D004792:Enzyme Precursors / Q000378:metabolism*; D066298:In Vitro Techniques; D007425:Intracellular Membranes / Q000378:metabolism; D008081:Liposomes; D008297:Male; D008930:Mitochondria, Liver / Q000378:metabolism*; D009953:Ornithine-Oxo-Acid Transaminase / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D013367:Submitochondrial Particles / Q000378:metabolism; D000637:Transaminases / Q000378:metabolism*
D002352:Carrier Proteins; D004792:Enzyme Precursors; D008081:Liposomes; D000637:Transaminases; D009953:Ornithine-Oxo-Acid Transaminase