A convenient and rapid method for the complete removal of CoA from butyryl-CoA dehydrogenase

Gary Williamson, Paul C. Engel

Research output: Contribution to journalArticleResearchpeer-review

15 Citations (Scopus)

Abstract

The commercially available gel, 2-pyridyl disulphide hydroxypropyl ether-Sepharose (thiopropyl-Sepharose 6B), can be used to remove bound ligand completely from butyryl-CoA dehydrogenase (EC 1.3.99.2) in two simple operations. The resultant enzyme forms normal complexes with acetoacetyl-CoA and CoA persulphide, contains no bound CoA as determined by the enzymatic assay for CoA, and retains full catalytic activity.

Original languageEnglish
Pages (from-to)245-248
Number of pages4
JournalBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Volume706
Issue number2
DOIs
Publication statusPublished - 7 Sep 1982
Externally publishedYes

Keywords

  • Butyryl-CoA dehydrogenase
  • CoA removal
  • Ligand removal
  • Thiopropyl-Sepharose 6B

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