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

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

doi:10.1016/0003-9861(80)90401-4

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 journal › Article › peer-review

14 Scopus citations

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	https://doi.org/10.1016/0003-9861(80)90401-4
State	Published - Jun 1980
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

Access to Document

10.1016/0003-9861(80)90401-4

Fingerprint Dive into the research topics of 'Stabilization of mammalian liver branched-chain α-ketoacid dehydrogenase by thiamin pyrophosphate'. Together they form a unique fingerprint.

Cite this

@article{d24d2801d5df40b787789472660d1315,

title = "Stabilization of mammalian liver branched-chain α-ketoacid dehydrogenase by thiamin pyrophosphate",

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.",

author = "Danner, {Dean J.} and Lemmon, {Sandra K.} and Elsas, {Louis J.}",

note = "Funding Information: We would like to thank Mrs. Mary Kroger for her expert technical assistance, Mrs. Carol Holman for typing this manuscript, and Dr. A. Sophianopoulos for his help with circular dichroism studies. This work was supported by Grant HD 08388 from the USPHS. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.",

year = "1980",

month = jun,

doi = "10.1016/0003-9861(80)90401-4",

language = "English (US)",

volume = "202",

pages = "23--28",

journal = "Archives of Biochemistry and Biophysics",

issn = "0003-9861",

publisher = "Academic Press Inc.",

number = "1",

}

TY - JOUR

T1 - Stabilization of mammalian liver branched-chain α-ketoacid dehydrogenase by thiamin pyrophosphate

AU - Danner, Dean J.

AU - Lemmon, Sandra K.

AU - Elsas, Louis J.

N1 - Funding Information: We would like to thank Mrs. Mary Kroger for her expert technical assistance, Mrs. Carol Holman for typing this manuscript, and Dr. A. Sophianopoulos for his help with circular dichroism studies. This work was supported by Grant HD 08388 from the USPHS. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.

PY - 1980/6

Y1 - 1980/6

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.

UR - http://www.scopus.com/inward/record.url?scp=0019023410&partnerID=8YFLogxK

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 -

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

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Cite this