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
I. Ghadiminejad et D. Saggerson, 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, International Journal of Biochemistry, 24(4), 1992, pp. 573-577
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.