Identical subcellular distribution of palmitoyl-CoA and arachidonoyl-CoA synthetase activities in human blood platelets

Biochem J. 1989 Jul 1;261(1):71-6. doi: 10.1042/bj2610071.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blood Platelets / enzymology*
  • Blood Platelets / ultrastructure
  • Coenzyme A Ligases / blood*
  • Enzyme Stability
  • Humans
  • Repressor Proteins*
  • Saccharomyces cerevisiae Proteins*
  • Subcellular Fractions / enzymology

Substances

  • Repressor Proteins
  • Saccharomyces cerevisiae Proteins
  • Coenzyme A Ligases
  • arachidonate - CoA ligase
  • FAA2 protein, S cerevisiae
  • long-chain-fatty-acid-CoA ligase