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Properties of component X of rat heart pyruvate dehydrogenase complex.

Authors :
Matuda S
Nakano K
Tabata I
Matuo S
Saheki T
Source :
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1988 Jan 29; Vol. 150 (2), pp. 816-21.
Publication Year :
1988

Abstract

Pyruvate dehydrogenase complex was purified from rat heart. A new component(mol.wt; 52,000) was found in the purified complex in addition to well known three component enzymes. This component(referred to as component X) was acetylated with [2-14C] pyruvate in the absence of CoA as well as lipoate acetyltransferase. The anti-lipoate acetyltransferase antibody reacted with component X and lipoate acetyltransferase, suggesting that component X shows homology with lipoate acetyltransferase in protein structure. cDNA for lipoate acetyltransferase was isolated from rat liver cDNA library in lambda gt 11. cDNA for lipoate acetyltransferase recognized two kinds of mRNAs of 3.5 Kb and 2.5 Kb.

Details

Language :
English
ISSN :
0006-291X
Volume :
150
Issue :
2
Database :
MEDLINE
Journal :
Biochemical and biophysical research communications
Publication Type :
Academic Journal
Accession number :
3342049
Full Text :
https://doi.org/10.1016/0006-291x(88)90464-0