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  • Title: Purification and properties of branched-chain alpha-keto acid dehydrogenase kinase from bovine kidney.
    Author: Lee HY, Hall TB, Kee SM, Tung HY, Reed LJ.
    Journal: Biofactors; 1991 Jun; 3(2):109-12. PubMed ID: 1910451.
    Abstract:
    Branched-chain alpha-keto acid dehydrogenase (BCKDH) kinase was purified 5000-fold to apparent homogeneity from extracts of bovine kidney mitochondria. The kinase co-purified with the BCKDH complex. About 70% of the kinase was released by treatment of the complex with 1.5 M NaCl and 0.1% 2-mercaptoethanol at pH 7.4, followed by chromatography on Sephacryl S-400. The uncomplexed kinase was purified further by chromatography on Q Sepharose and Superose 12. The purified kinase is a monomer of apparent Mr approximately 43,000. BCKDH kinase exhibited little activity, if any, toward pyruvate dehydrogenase.
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