Immunochemical comparison of lipoamide dehydrogenases from various sources and reactivity of various lipoamide dehydrogenases with rat heart pyruvate dehydrogenase-subcomplex.
Lipoamide dehydrogenases from various sources were purified and their immunochemical properties were compared. Antibody against rat lipoamide dehydrogenase reacted with rat, human, pig, pigeon and frog enzymes, but not with enzymes from E. coli, yeast and Ascaris. Anti-Ascaris enzyme and anti-E. coli enzyme antibodies reacted with Ascaris and E. coli enzymes, respectively. The pyruvate dehydrogenase subcomplex, which consists of pyruvate dehydrogenase and lipoate acetyltransferase, was prepared by releasing the lipoamide dehydrogenase from rat heart pyruvate dehydrogenase complex by anti-lipoamide dehydrogenase antibody. Lipoamide dehydrogenases from various sources were added to rat pyruvate dehydrogenase subcomplex and the complex overall activity was measured. Each lipoamide dehydrogenase effectively recovered the overall activity of rat pyruvate dehydrogenase subcomplex to 80% of the original activity.
D000818:Animals; D001200:Ascaris / Q000201:enzymology; D003429:Cross Reactions; D008058:Dihydrolipoamide Dehydrogenase / Q000276:immunology*; D004926:Escherichia coli / Q000201:enzymology; D006801:Humans; D007120:Immunochemistry; D008970:Molecular Weight; D009206:Myocardium / Q000201:enzymology*; D011768:Pyruvate Dehydrogenase Complex / Q000276:immunology*; D051381:Rats; D013045:Species Specificity
D011768:Pyruvate Dehydrogenase Complex; D008058:Dihydrolipoamide Dehydrogenase