Purification and properties of branched-chain alpha-keto acid dehydrogenase kinase from bovine kidney |
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| Authors: | H Y Lee T B Hall S M Kee H Y Tung L J Reed |
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| Affiliation: | Clayton Foundation Biochemical Institute, Austin, TX. |
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| 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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