Immunochemical identification of branched-chain 2-oxo acid dehydrogenase kinase

Yoshiharu Shimomura, Noriko Nanaumi, Masashige Suzuki, Robert A. Harris

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Abstract

Branched-chain 2-oxo acid dehydrogenase kinase was characterized using anti-kinase polygonal antibodies. The antibodies were purified from rabbit antiserum by an epitope selection method. The antibodies bound only to a 44 kDa polypeptide in the dehydrogenase-kinase complex and inhibited the kinase activity, substantiating that the 44 kDa polypeptide is the catalytic subunit of the kinase. The purified liver dehydrogenase-kinase complex, but not either the purified heart complex or the partially purified liver complex, contained 2 additional polypeptides of lower molecular weight which also reacted with the anti-kinase antibodies, suggesting that the liver kinase is subject to proteolytic degradation during purification.

Original languageEnglish (US)
Pages (from-to)95-97
Number of pages3
JournalFEBS Letters
Volume288
Issue number1-2
DOIs
StatePublished - Aug 19 1991

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Keywords

  • Anti-kinase antibody
  • Branched-chain 2-oxo acid dehydrogenase complex
  • Branched-chain 2-oxo acid dehydrogenase kinase
  • Low-protein fed rat
  • Rat heart
  • Rat liver

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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