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PMID: 2932110 Published · ppublish English Journal Article

Identification of a cDNA clone in lambda gt11 for the transacylase component of branched chain ketoacid dehydrogenase.

Biochemical and biophysical research communications ·Vol. 131 ·No. 2 ·1985-09-16 ·Pages 961-7

Litwer S, Danner DJ

Abstract

Two cDNA clones for the transacylase protein of the branched chain ketoacid dehydrogenase complex [E.C. 1.2.4.4] have been isolated from a human fetal liver cDNA expression library in lambda gt11 using antibody selection. By selective antibody elution from nitrocellulose filters containing the fusion proteins, it was determined that these inserts represent the transacylase protein. These data support the hypothesis that this protein is synthesized in the cytosol on transcripts independent of the other proteins of the branched chain ketoacid dehydrogenase complex.

MeSH Terms
3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) Animals Bacteriophage lambda/genetics Collodion DNA/genetics,isolation & purification DNA, Recombinant Humans Immunologic Techniques Ketone Oxidoreductases/genetics Liver/analysis,embryology Mice Mitochondria, Liver/analysis Multienzyme Complexes/genetics
Chemicals
DNA, Recombinant Multienzyme Complexes Collodion DNA Ketone Oxidoreductases 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Litwer S
Danner D J
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1985-09-16
Pages
961-7
Language
English
Region
United States
NLM ID
0372516
Subset
IM
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