Immunochemical identification of branched‐chain 2‐oxo acid dehydrogenase kinase

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Abstract
Branched‐chain 2‐oxo acid dehydrogenase kinase was characterized using anti‐kinase polygonal 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.