USE OF MITOCHONDRIAL INNER MEMBRANE-PROTEINS AND PHOSPHOLIPIDS TO FACILITATE DISENGAGEMENT OF THE CATALYTIC AND MALONYL-COA BINDING-COMPONENTS OF CARNITINE PALMITOYLTRANSFERASE FROM LIVER MITOCHONDRIAL OUTER MEMBRANES

1. It was shown by Ghadiminejad and Saggerson (1991) that the anionic detergent cholate caused disengagement of the malonyl-CoA binding enti ty from the catalytic entity of outer membrane carnitine palmitoyltran sferase (CPT1). 2. This disengagement was only observed if inner membr ane material was present. 3. It is now shown that this effect is mimic ked by a CPT-free inner membrane protein fraction together with an inn er membrane lipid extract or with individual phospholipids (phosphatid ylcholine, phosphatidylethanolamine or diphosphatidylglycerol). 4. The lipids alone have no effect but act synergistically with the inner me mbrane protein fraction.