Carnitine palmitoyltransferase: separation of enzyme activity and malonyl-CoA binding in rat liver mitochondria.
Carnitine palmitoyltransferase activity and malonyl-CoA binding capacity have been studied in Triton X-100 extracts and membrane residues of rat liver mitochondria. Rat liver mitochondria extracted twice with 0.5% Triton X-100 in a salt-free medium showed increased specific binding of [2-14C]malonyl-CoA when compared with intact mitochondria. High malonyl-CoA binding required the presence of salts and was inhibited by albumin. Further solubilization of the membrane residues in the Triton/KCl medium and subsequent hydroxylapatite chromatography gave a complete separation of carnitine palmitoyltransferase and malonyl-CoA binding. The results show that malonyl-CoA binds to mitochondrial component(s) which is different from and  more difficult to extract from the mitochondrial membrane than most of the carnitine palmitoyltransferase.
D000214:Acyl Coenzyme A / Q000378:metabolism*; D000217:Acyltransferases / Q000302:isolation & purification*; D000418:Albumins / Q000494:pharmacology; D000818:Animals; D002250:Carbon Radioisotopes; D002334:Carnitine O-Palmitoyltransferase / Q000302:isolation & purification*; D066298:In Vitro Techniques; D008297:Male; D008316:Malonyl Coenzyme A / Q000378:metabolism*; D008930:Mitochondria, Liver / Q000201:enzymology*; D011189:Potassium Chloride / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains
D000214:Acyl Coenzyme A; D000418:Albumins; D002250:Carbon Radioisotopes; D008316:Malonyl Coenzyme A; D011189:Potassium Chloride; D000217:Acyltransferases; D002334:Carnitine O-Palmitoyltransferase