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

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

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

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
Pages (from-to)23-28
Number of pages6
JournalArchives of Biochemistry and Biophysics
Volume202
Issue number1
DOIs
StatePublished - Jan 1 1980
Externally publishedYes

Fingerprint

3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)
Thiamine Pyrophosphate
Liver
Stabilization
Circular dichroism spectroscopy
Chymotrypsin
Coenzyme A
Circular Dichroism
NAD
Half-Life
Spectrum Analysis
Hot Temperature
Membranes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Stabilization of mammalian liver branched-chain α-ketoacid dehydrogenase by thiamin pyrophosphate. / Danner, Dean J.; Lemmon, Sandra; Elsas, Louis J.

In: Archives of Biochemistry and Biophysics, Vol. 202, No. 1, 01.01.1980, p. 23-28.

Research output: Contribution to journalArticle

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