Lignoceroyl-coenzyme A synthetase from developing rat brain: partial purification, characterization and comparison with palmitoyl-coenzyme A synthetase activity and liver enzyme

Biochim Biophys Acta. 1985 Aug 22;836(1):80-8. doi: 10.1016/0005-2760(85)90223-1.


As part of a long-term study of sphingolipid metabolism in brain, we have purified and partially characterized a long-chain acyl-CoA synthetase from microsomes of developing rat brain and compared it with the hepatic microsomal enzyme from the same animals. Both enzymes were solubilized from microsomes by treatment with Triton X-100 and then chromatographed successively on Blue-Sepharose and DEAE-Sepharose. Blue-Sepharose chromatography yielded a single peak with acyl-CoA synthetase activity, whereas DEAE-Sepharose chromatography of both brain and liver preparations yielded two peaks. Elution patterns of lignoceroyl-CoA synthetase and palmitoyl-CoA synthetase activities were identical throughout these steps and were similar in brain and liver. Gel filtration of each DEAE-Sepharose fraction on Sephadex G-200 also yielded two peaks of activity. The more rapidly eluted material contained much more lignoceroyl-CoA synthetase activity, while the activity for palmitoyl-CoA synthetase was higher in slower eluting peaks. In all preparations the ratio of lignoceroyl-CoA synthetase activity to palmitoyl-CoA synthetase activity was much higher in brain than in liver. These results suggest that although the brain acyl-CoA synthetase is chromatographically similar to the liver enzyme, there are differences in substrate specificity.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Brain / enzymology*
  • Brain / ultrastructure
  • Chromatography, Gel
  • Chromatography, Ion Exchange
  • Chromatography, Thin Layer
  • Coenzyme A Ligases / metabolism*
  • Microsomes / enzymology
  • Microsomes, Liver / enzymology*
  • Octoxynol
  • Polyethylene Glycols / pharmacology
  • Rats
  • Rats, Inbred Strains
  • Repressor Proteins*
  • Saccharomyces cerevisiae Proteins*
  • Solubility


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