Comparison of the binding affinities of acyl-CoA-binding protein and fatty-acid-binding protein for long-chain acyl-CoA esters.
Bovine and rat liver acyl-CoA-binding proteins (ACBP) were found to exhibit a much higher affinity for long-chain acyl-CoA esters than both bovine hepatic and cardiac fatty-acid-binding proteins (hFABP and cFABP respectively). In the Lipidex 1000- as well as the liposome-binding assay, bovine and rat hepatic ACBP effectively bound long-chain acyl-CoA ester, h- and c-FABP were, under identical conditions, unable to bind significant amounts of long-chain acyl-CoA esters. When FABP, ACBP and [1-14C]hexadecanoyl-CoA were mixed, hexadecanoyl-CoA could be shown to be bound to ACBP only. The experimental results give strong evidence that ACBP, and not FABP, is the predominant carrier of acyl-CoA in liver.
Rasmussen
J T
JT
Institute of Biochemistry, Odense University, Denmark.
Börchers
T
T
Knudsen
J
J
D000214:Acyl Coenzyme A / Q000378:metabolism*; D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification / Q000378:metabolism*; D002417:Cattle; D026261:Diazepam Binding Inhibitor; D004591:Electrophoresis, Polyacrylamide Gel; D004952:Esters / Q000378:metabolism; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D005227:Fatty Acids / Q000378:metabolism*; D008862:Microsomes, Liver / Q000378:metabolism; D009206:Myocardium / Q000378:metabolism; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; D051381:Rats; D011919:Rats, Inbred Strains; D012709:Serum Albumin / Q000378:metabolism
D000214:Acyl Coenzyme A; D002352:Carrier Proteins; D026261:Diazepam Binding Inhibitor; D004952:Esters; C490174:Fabp7 protein, rat; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D005227:Fatty Acids; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; D012709:Serum Albumin