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 language | English (US) |
|---|---|
| Pages (from-to) | 23-28 |
| Number of pages | 6 |
| Journal | Archives of Biochemistry and Biophysics |
| Volume | 202 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jun 1980 |
| Externally published | Yes |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
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Cite this
Danner, D. J., Lemmon, S. K., & Elsas, L. J. (1980). Stabilization of mammalian liver branched-chain α-ketoacid dehydrogenase by thiamin pyrophosphate. Archives of Biochemistry and Biophysics, 202(1), 23-28. https://doi.org/10.1016/0003-9861(80)90401-4