Rat liver microsomal palmitoyl-coenzyme A synthetase. Structural properties

Biochem J. 1973 Mar;131(3):443-9. doi: 10.1042/bj1310443.

Abstract

The structural properties of purified palmitoyl-CoA synthetase from rat liver microsomal material were investigated. The active enzyme has a molecular weight of 168000 and contains about 8.2mol of phospholipid bound/mol of enzyme protein, as well as bound fatty acids. Association of the active enzyme was shown to occur, without impairment of catalytic activity. The lowest-molecular-weight species obtained under denaturing conditions was 27000 daltons.

MeSH terms

  • Amino Acids / analysis
  • Animals
  • Chemical Phenomena
  • Chemistry
  • Chromatography, Gel
  • Coenzyme A Ligases* / analysis
  • Electrophoresis, Polyacrylamide Gel
  • Isoelectric Focusing
  • Lipids / analysis
  • Macromolecular Substances
  • Microsomes, Liver / enzymology*
  • Molecular Weight
  • Palmitic Acids
  • Phospholipids / analysis
  • Protein Binding
  • Protein Denaturation
  • Rats
  • Sodium Dodecyl Sulfate
  • Tritium
  • Ultracentrifugation

Substances

  • Amino Acids
  • Lipids
  • Macromolecular Substances
  • Palmitic Acids
  • Phospholipids
  • Tritium
  • Sodium Dodecyl Sulfate
  • Coenzyme A Ligases