Acyl-CoA-binding protein (ACBP) can mediate intermembrane acyl-CoA transport and donate acyl-CoA for beta-oxidation and glycerolipid synthesis
Research output: Contribution to journal › Journal article › Research › peer-review
The dissociation constants for octanoyl-CoA, dodecanoyl-CoA and hexadecanoyl-CoA binding to acyl-CoA-binding protein (ACBP) were determined by using titration microcalorimetry. The KD values obtained, (0.24 +/- 0.02) x 10(-6) M, (0.65 +/- 0.2) x 10(-8) M and (0.45 +/- 0.2) x 10(-13) M respectively, were much lower than expected. ACBP was able to extract hexadecanoyl-CoA from phosphatidylcholine membranes immobilized on a nitrocellulose membrane. The acyl-CoA/ACBP complex formed was able to transport acyl-CoA to mitochondria or microsomes in suspension, or to microsomes immobilized on a nitrocellulose membrane, and to donate them to beta-oxidation or glycerolipid synthesis in mitochondria or microsomes, respectively.
|Volume||299 ( Pt 1)|
|Number of pages||5|
|Publication status||Published - 1994|
Keywords: Acyl Coenzyme A; Animals; Biological Transport; Calorimetry; Carrier Proteins; Cattle; Diazepam Binding Inhibitor; Female; Glycerides; Intracellular Membranes; Male; Microsomes; Mitochondria; Oxidation-Reduction; Rabbits; Rats