Immunochemical identification of branched-chain 2-oxo acid dehydrogenase kinase.
Branched-chain 2-oxo acid dehydrogenase kinase was characterized using anti-kinase polyclonal antibodies. The antibodies were purified from rabbit antiserum by an epitope selection method. The antibodies bound only to a 44 kDa polypeptide in the dehydrogenase-kinase complex and inhibited the kinase activity, substantiating that the 44 kDa polypeptide is the catalytic subunit of the kinase. The purified liver dehydrogenase-kinase complex, but not either the purified heart complex or the partially purified liver complex, contained 2 additional polypeptides of lower molecular weight which also reacted with the anti-kinase antibodies, suggesting that the liver kinase is subject to proteolytic degradation during purification.
Shimomura
Y
Y
Laboratory of Biochemistry of Exercise and Nutrition, University of Tsukuba, Ibaraki, Japan.
Nanaumi
N
N
Suzuki
M
M
Harris
R A
RA
D042942:3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide); D000818:Animals; D000911:Antibodies, Monoclonal; D015153:Blotting, Western; D007658:Ketone Oxidoreductases / Q000276:immunology / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D009097:Multienzyme Complexes / Q000276:immunology / Q000378:metabolism*; D009206:Myocardium / Q000201:enzymology; D011494:Protein Kinases / Q000276:immunology* / Q000302:isolation & purification / Q000378:metabolism; D051381:Rats
D000911:Antibodies, Monoclonal; D009097:Multienzyme Complexes; D007658:Ketone Oxidoreductases; D042942:3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide); D011494:Protein Kinases