Purification of branched chain α-ketoacid dehydrogenase complex from rat liver

Yoshiharu Shimomura, Ralph Paxton, Takayuki Ozawa, Robert A. Harris

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29 Scopus citations


A new method using hydrophobic interaction chromatography on phenyl-Sepharose was developed to purify branched chain α-ketoacid dehydrogenase complex from commercially available frozen rat liver. Yields of greater than 50% were routinely achieved. The purified enzyme, composed of E1α, E1β, and E2 subunits, appeared homogeneous on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and contained endogenous kinase activity for phosphorylation and inactivation of the complex.

Original languageEnglish (US)
Pages (from-to)74-78
Number of pages5
JournalAnalytical biochemistry
Issue number1
StatePublished - May 15 1987



  • branched chain α-ketoacid dehydrogenase complex
  • branched chain α-ketoacid dehydrogenase kinase
  • hydrophobic interaction chromatography
  • rat liver

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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