Identical subcellular distribution of palmitoyl-CoA and arachidonoyl-CoA synthetase activities in human blood platelets.
Fractionation of human blood platelets showed that palmitoyl-CoA synthetase and arachidonoyl-CoA synthetase activities had an identical distribution among subcellular fractions. The activity was highest with arachidonic acid as substrate in all fractions, with an enzyme activity of 50 nmol/min per mg of protein, in a 'dense-tubular-system'-enriched fraction. The ratio activities with arachidonate and palmitate as substrates was about 1.5 in all fractions. Heat inactivation did not distinguish between arachidonoyl-CoA synthetase and a palmitoyl-CoA synthetase. On the other hand, heat inactivation indicated two pools of long-chain acyl-CoA synthetases: one in a mitochondria- and one in the dense-tubular-system-enriched fraction.
Bakken
A M
AM
Laboratory of Clinical Biochemistry, University of Bergen, University Hospital Haukeland, Norway.
Farstad
M
M
D001792:Blood Platelets / Q000201:enzymology* / Q000648:ultrastructure; D003066:Coenzyme A Ligases / Q000097:blood*; D004795:Enzyme Stability; D006801:Humans; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D013347:Subcellular Fractions / Q000201:enzymology; D000098859:Long-Chain-Fatty-Acid-CoA Ligase
D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D003066:Coenzyme A Ligases; C033896:arachidonate - CoA ligase; C090799:FAA2 protein, S cerevisiae; D000098859:Long-Chain-Fatty-Acid-CoA Ligase