Identification of a cDNA clone in lambda gt11 for the transacylase component of branched chain ketoacid dehydrogenase.
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.
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D042942:3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide); D000818:Animals; D010582:Bacteriophage lambda / Q000235:genetics*; D003101:Collodion; D004247:DNA / Q000235:genetics / Q000302:isolation & purification*; D004274:DNA, Recombinant; D006801:Humans; D007158:Immunologic Techniques; D007658:Ketone Oxidoreductases / Q000235:genetics*; D008099:Liver / Q000032:analysis / Q000196:embryology; D051379:Mice; D008930:Mitochondria, Liver / Q000032:analysis; D009097:Multienzyme Complexes / Q000235:genetics*
D004274:DNA, Recombinant; D009097:Multienzyme Complexes; D003101:Collodion; D004247:DNA; D007658:Ketone Oxidoreductases; D042942:3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)