Stabilization of mammalian liver branched-chain α-ketoacid dehydrogenase by thiamin pyrophosphate

Dean J. Danner, Sandra K. Lemmon, Louis J. Elsas

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


Thiamin pyrophosphate, CoASH, and NAD+ have been shown to reversibly bind to the purified bovine liver mitochondrial branched-chain α-ketoacid dehydrogenase complex. When saturated with thiamin pyrophosphate, the complex was more stable to heat and chymotrypsin inactivation. Under identical saturating conditions a conformational change in the complex was observed by circular dichroism spectroscopy. We postulate that thiamin pyrophosphate can increase the biological half-life of the in vivo, membrane-bound complex through conformational changes induced by the binding of this cofactor.

Original languageEnglish (US)
Pages (from-to)23-28
Number of pages6
JournalArchives of Biochemistry and Biophysics
Issue number1
StatePublished - Jun 1980
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


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