Fatty acyl-CoA dehydrogenase enzymes in human skeletal muscle

James E. Carroll, Byron S. McGuire, Carole L. Hall

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


An electrophoretic and enzyme-substrate staining technique for acyl-CoA dehydrogenase (ACD) enzymes was developed for use with small (< 100 mg) tissue samples. Based on their electrophoretic mobility and substrate staining specificity, at least two and perhaps three chain-length specific enzymes for dehydrogenation of saturated fatty acids were found in human skeletal muscle. ACD enzymes staining with octanoyl-CoA or palmitoyl-CoA were identified by this technique in human skeletal muscle, heart, and liver, but the ACD enzyme staining with butyryl-CoA was difficult to detect and was definitely visualized only in skeletal muscle.

Original languageEnglish (US)
Pages (from-to)327-333
Number of pages7
JournalClinica Chimica Acta
Issue number3
StatePublished - Dec 30 1986


  • Acyl-CoA dehydrogenase
  • Heart
  • Liver
  • Skeletal muscle

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Biochemistry, medical


Dive into the research topics of 'Fatty acyl-CoA dehydrogenase enzymes in human skeletal muscle'. Together they form a unique fingerprint.

Cite this