Abstract

Mitochondrial thioesterase from rabbit myocardium was purified to homogeneity by sequential ion exchange, hydroxylapatite, chromatofocusing and gel filtration chromatographies. The purified protein had an apparent molecular mass of 170 kDa. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and subsequent silver staining revealed a single band (Mr 43 000) demonstrating that the protein is a tetramer. The specific activity of the purifed thioesterase for palmitoyl-CoA hydrolysis was 1.8 μmol/mg per min. Thioesterase activity was maximal at pH 8 and was activated by Mg2+ but inhibited by Ca2+. Pathophysiological concentrations of L-palmitoyl carnitine (20-400 μM) competitively inhibited enzymic activity. The purified enzyme was also inhibited by high concentrations of substrate (over 20 μM palmitoyl-CoA).

Original languageEnglish
Pages (from-to)197-202
Number of pages6
JournalBBA - General Subjects
Volume802
Issue number2
DOIs
StatePublished - Nov 28 1984

Keywords

  • (Rabbit myocardium)
  • Palmitoyl carnitine
  • Thiolesterase inhibition

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