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 |
|---|---|
| Pages (from-to) | 23-28 |
| Number of pages | 6 |
| Journal | Archives of Biochemistry and Biophysics |
| Volume | 202 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 1 1980 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
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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 journal › Article
}
TY - JOUR
T1 - Stabilization of mammalian liver branched-chain α-ketoacid dehydrogenase by thiamin pyrophosphate
AU - Danner, Dean J.
AU - Lemmon, Sandra
AU - Elsas, Louis J.
PY - 1980/1/1
Y1 - 1980/1/1
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0019023410&partnerID=8YFLogxK
U2 - 10.1016/0003-9861(80)90401-4
DO - 10.1016/0003-9861(80)90401-4
M3 - Article
C2 - 7396533
AN - SCOPUS:0019023410
VL - 202
SP - 23
EP - 28
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
IS - 1
ER -